Caveolin-1 is an oligomeric membrane protein that forms the membrane-embedded structural framework of caveolae together with CAV2 and cavin partners. Its tightly associated protomers support a stable coat that can insert into the cytoplasmic membrane leaflet. Separate interactions organize selected receptors, channels and trafficking proteins, while direct inhibition of nitric-oxide synthase provides a defined enzyme-regulatory activity. Partner recruitment and regulatory direction depend on the cellular context, phosphorylation and relative protein abundance. The alpha and beta products arise from alternative translation initiation. Biallelic loss of CAV1 causes generalized lipodystrophy, and heterozygous variants are associated with incompletely penetrant pulmonary arterial hypertension; evidence for dominant lipodystrophy and amyotrophic lateral sclerosis is more limited.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000122 negative regulation of transcription by RNA polymerase II | IEA GO_REF:0000107 | UNDECIDED | Summary: The particular transcriptional repression mechanism remains unresolved. Reason: The mouse CAV1 ortholog is the specified donor. Membrane signaling can change transcription, but that alone does not identify the experimentally supported RNA-polymerase-II repression mechanism underlying this transfer. The original donor assay and context have not been resolved; this is not evidence of a false orthology assignment. |
| GO:0000122 negative regulation of transcription by RNA polymerase II | ISS GO_REF:0000024 | UNDECIDED | Summary: The particular transcriptional repression mechanism remains unresolved. Reason: The mouse CAV1 ortholog is the specified donor. Membrane signaling can change transcription, but that alone does not identify the experimentally supported RNA-polymerase-II repression mechanism underlying this transfer. The original donor assay and context have not been resolved; this is not evidence of a false orthology assignment. |
| GO:0000139 Golgi membrane | IDA PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | KEEP AS NON CORE | Summary: Golgi-membrane localization is retained as a trafficking context. Reason: The BENE study describes human ECV304 raft trafficking and intracellular CAV1-containing structures. The exact Golgi localization experiment is not visible in the cached abstract; independently established Golgi passage and the experimental curator support retention, without claiming the compartment marker was re-read. |
| GO:0000139 Golgi membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: The Golgi membrane is a supported intracellular CAV1 pool. Reason: The source translates a reviewed UniProt subcellular-location assertion rather than a new imaging experiment. Golgi trafficking is consistent with the reviewed protein record; it is secondary to the plasma-membrane caveolar activity. Supporting Evidence: UniProt:Q03135 |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-204549 | KEEP AS NON CORE | Summary: Retain the Golgi context of the curated basigin association. Reason: The complete Reactome summary describes CAV1 association with basigin during Golgi trafficking. This supports compartmental residence, not matrix-metalloprotease catalysis by CAV1. Supporting Evidence: Reactome:R-HSA-204549 |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9021068 | KEEP AS NON CORE | Summary: Retain the Golgi trafficking pool associated with estrogen receptor. Reason: The curated events describe palmitoylated estrogen receptor association with CAV1 and its transport from the Golgi toward the plasma membrane. They support this localization without making CAV1 an estrogen receptor or a palmitoyltransferase. Supporting Evidence: Reactome:R-HSA-9021068 Reactome:R-HSA-9021079 |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9021079 | KEEP AS NON CORE | Summary: Retain the Golgi trafficking pool associated with estrogen receptor. Reason: The curated events describe palmitoylated estrogen receptor association with CAV1 and its transport from the Golgi toward the plasma membrane. They support this localization without making CAV1 an estrogen receptor or a palmitoyltransferase. Supporting Evidence: Reactome:R-HSA-9021068 Reactome:R-HSA-9021079 |
| GO:0000139 Golgi membrane | TAS Reactome:R-HSA-9731034 | KEEP AS NON CORE | Summary: Golgi localization is retained in the viral-protein interaction context. Reason: The Reactome event describes CAV1 association with SARS-CoV-1 ORF3a at the Golgi. This context does not transfer ORF3a ion-channel activity to CAV1. Supporting Evidence: Reactome:R-HSA-9731034 |
| GO:0001570 vasculogenesis | ISS GO_REF:0000024 | UNDECIDED | Summary: Vasculogenesis requires a source-specific donor audit. Reason: The exact mouse donor experiment separating vessel formation from later vascular maintenance or endothelial signaling was not resolved. Vascular disease and endothelial CAV1 expression alone do not settle this particular developmental process. |
| GO:0001666 response to hypoxia | ISS GO_REF:0000024 | UNDECIDED | Summary: The transferred hypoxia response remains context dependent. Reason: The specified mouse donor is credible, but the underlying hypoxia perturbation and response endpoint were not accessed. Hyperoxia experiments elsewhere in this review are not interchangeable evidence for hypoxia. |
| GO:0001937 negative regulation of endothelial cell proliferation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the inherited endothelial proliferation phenotype as non-core. Reason: The PAINT assertion describes a regulatory consequence of caveolin signaling, not a separate CAV1 catalytic activity. It is retained with curator deference; the ancestral node and alignment were not independently inspected, and no node-placement failure is asserted. |
| GO:0001937 negative regulation of endothelial cell proliferation | ISS GO_REF:0000024 | UNDECIDED | Summary: The mouse-to-human endothelial proliferation transfer is not independently resolved. Reason: The precise donor perturbation, endothelial model and proliferation assay remain uninspected. The credible related PAINT assertion does not replace evaluation of this distinct transfer provenance. |
| GO:0002080 acrosomal membrane | IEA GO_REF:0000107 | UNDECIDED | Summary: The acrosomal membrane transfer remains unresolved. Reason: Mouse Cav1 is the specified ortholog donor, not a demonstrated human sperm localization assay. The exact donor imaging and compartment controls were not accessed. The annotation is preserved without a claim of a paralog error. |
| GO:0002095 caveolar macromolecular signaling complex | IEA GO_REF:0000107 | ACCEPT | Summary: CAV1 organizes caveolar signaling assemblies. Reason: Direct CAV1 association and recruitment experiments, together with caveolin-cavin coat isolation, support participation in caveolar macromolecular assemblies. These do not imply that all signaling partners are stable constituents of a single fixed stoichiometric complex. |
| GO:0005102 signaling receptor binding | IPI PMID:16890161 Caveolin is necessary for Wnt-3a-dependent internalization o... | KEEP AS NON CORE | Summary: LRP6 association is a supported receptor-binding context. Reason: The complete abstract reports LRP6 binding to CAV1 and Wnt-dependent receptor internalization. This is a receptor-trafficking interaction, not Wnt ligand activity or receptor catalysis by CAV1. Supporting Evidence: |
| GO:0005113 patched binding | NAS PMID:11278759 The sonic hedgehog receptor patched associates with caveolin... | KEEP AS NON CORE | Summary: Patched association is supported as a specific partner interaction. Reason: The primary abstract reports CAV1 association with Patched in cholesterol-rich membrane domains. The linked correction changes an author-name spelling only. The record does not establish that CAV1 supplies Hedgehog ligand activity or universally activates Patched. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10212252 Flotillins/cavatellins are differentially expressed in cells... | KEEP AS NON CORE | Summary: CAV2 coassociation is retained. Reason: The original flotillin-focused abstract does not expose the individual CAV1-CAV2 assay. Independent human caveolar-coat isolation and the exact reviewed UniProt edge support this association; neither a fixed dimer nor a direct interface is inferred. |
| GO:0005515 protein binding | IPI PMID:11075810 Constitutive and growth factor-regulated phosphorylation of ... | KEEP AS NON CORE | Summary: Phosphorylated CAV1 associates with Grb7. Reason: The complete source abstract reports Tyr14-dependent Grb7 association in vitro and in cells. The preserved Q03160 partner is mouse Grb7 in the UniProt xenointeraction record. The exact species of every construct and domain-level assay were not rechecked, so retain the generic association without inventing a human partner or an SH2 assay. |
| GO:0005515 protein binding | IPI PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | KEEP AS NON CORE | Summary: BENE associates with CAV1 during membrane trafficking. Reason: The source describes BENE and caveolin-associated membrane trafficking. Retain the exact Q13021 partner and curated association without assigning BENE trafficking functions to CAV1 or claiming a purified binding interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:12176037 Some protein tyrosine phosphatases target in part to lipid r... | MODIFY | Summary: Refine PTP1B association to protein phosphatase binding. Reason: The complete abstract explicitly reports coimmunoprecipitation of PTP1B and four other phosphatases with CAV1, beyond simple motif prediction or co-fractionation. This supports binding to the specified P18031 phosphatase. It does not make CAV1 a phosphatase or establish activation of that enzyme. Proposed replacements: protein phosphatase binding Supporting Evidence: PMID:12176037 all five phosphatases form molecular complexes with caveolin-1 in vivo |
| GO:0005515 protein binding | IPI PMID:15182174 Sterol carrier protein-2 directly interacts with caveolin-1 ... | KEEP AS NON CORE | Summary: SCP2 association is supported. Reason: The source reports FRET, coimmunoprecipitation and two-hybrid evidence for the specified sterol-carrier protein association, with a distinct phosphatidylinositol-transfer-protein comparison. This is a binding context, not lipid-transfer catalysis by CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15504032 Tyrosine phosphorylation of caveolin-2 at residue 27: differ... | KEEP AS NON CORE | Summary: Retain the curated CAV1-RASA1 association. Reason: The CAV2-focused abstract does not resolve this particular CAV1 target assay. The exact P20936 interaction is independently recorded in reviewed UniProt; retain qualitative binding with curator deference, without claiming the original source table or direct interface was inspected. Supporting Evidence: UniProt:Q03135 |
| GO:0005515 protein binding | IPI PMID:15657067 Phosphotyrosine signaling networks in epidermal growth facto... | KEEP AS NON CORE | Summary: Retain the supported EGFR association. Reason: The source uses EGFR affinity-purification proteomics; its individual CAV1 target row was not independently inspected. The exact EGFR edge in reviewed UniProt and the separate CAV1-EGFR association discussion support retention without assigning a kinase activity to CAV1. |
| GO:0005515 protein binding | IPI PMID:15703204 Maxi-K channels localize to caveolae in human myometrium: a ... | MODIFY | Summary: Refine the maxi-K channel interaction to transporter binding. Reason: Human myometrial coimmunoprecipitation, colocalization and caveolar localization support the CAV1-KCNMA1 association in the complete abstract. The specified partner is a membrane channel; conductance remains the partner activity. Proposed replacements: transmembrane transporter binding Supporting Evidence: PMID:15703204 maxi-K channels associate and colocalize with caveolar scaffolding proteins caveolin-1 and caveolin-2 |
| GO:0005515 protein binding | IPI PMID:16388599 Identification of phosphocaveolin-1 as a novel protein tyros... | MODIFY | Summary: Refine the phosphatase-substrate association to phosphatase binding. Reason: The complete abstract reports physical PTP1B-CAV1 association, substrate-trapping D181A and dephosphorylation controls. CAV1 is the phosphoprotein substrate in these experiments, not the phosphatase or a demonstrated phosphatase activator. Proposed replacements: protein phosphatase binding Supporting Evidence: PMID:16388599 PTP1B physically associates with caveolin-1 |
| GO:0005515 protein binding | IPI PMID:16799092 Dynamic profiling of the post-translational modifications an... | KEEP AS NON CORE | Summary: Retain EGFR coassociation with source-specific limits. Reason: The EGFR proteomic study does not expose its individual CAV1 assay in the abstract. The exact curated EGFR interaction and independent CAV1-EGFR source discussion support qualitative retention; no source-table validation or kinase regulation is claimed. |
| GO:0005515 protein binding | IPI PMID:16890161 Caveolin is necessary for Wnt-3a-dependent internalization o... | KEEP AS NON CORE | Summary: Retain the curated Axin1 xenointeraction. Reason: The Wnt/LRP6 study concerns recruitment and receptor internalization. Reviewed UniProt independently records the exact O70239 mouse Axin1 partner as a xenointeraction. The original pair-specific construct and interaction controls remain uninspected; this does not license replacing the source partner with human AXIN1. Supporting Evidence: UniProt:Q03135 |
| GO:0005515 protein binding | IPI PMID:16890161 Caveolin is necessary for Wnt-3a-dependent internalization o... | KEEP AS NON CORE | Summary: LRP6 association is retained as a receptor interaction. Reason: The complete abstract explicitly reports LRP6 binding to CAV1 during Wnt-dependent internalization. This supports the receptor-associated complex without transferring receptor signaling or ligand activity to CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16951145 Interaction of deleted in liver cancer 1 with tensin2 in cav... | KEEP AS NON CORE | Summary: Retain the DLC1/tensin2-associated interaction. Reason: The complete abstract identifies CAV1-binding motifs and reports immunoprecipitation of both DLC1 and tensin2 with endogenous CAV1. These complex associations are distinct from the reported direct DLC1-tensin2 interaction and do not make CAV1 a RhoGAP. The exact source partner is preserved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16951145 Interaction of deleted in liver cancer 1 with tensin2 in cav... | KEEP AS NON CORE | Summary: Retain the DLC1/tensin2-associated interaction. Reason: The complete abstract identifies CAV1-binding motifs and reports immunoprecipitation of both DLC1 and tensin2 with endogenous CAV1. These complex associations are distinct from the reported direct DLC1-tensin2 interaction and do not make CAV1 a RhoGAP. The exact source partner is preserved. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17287217 Caveolin-1 triggers T-cell activation via CD26 in associatio... | KEEP AS NON CORE | Summary: CD26/DPP4 association is supported. Reason: The complete source abstract describes CAV1 interaction with CD26/DPP4 in the T-cell costimulation context. Retain qualitative association without assigning DPP4 peptidase activity or a universal costimulatory role to CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17848177 Tissue factor induction by protease-activated receptor 1 req... | KEEP AS NON CORE | Summary: PAR1 association is retained. Reason: The receptor-partner relationship is independently supported by reciprocal PAR1-CAV1 immunoprecipitation in the later endothelial-cell study. The original source assay is not fully re-read; retention does not mean CAV1 cleaves or activates PAR1 enzymatically. |
| GO:0005515 protein binding | IPI PMID:17855368 Identification of a novel inhibitor of differentiation-1 (ID... | KEEP AS NON CORE | Summary: ID1 association is supported in the tested cancer-cell setting. Reason: The complete abstract reports two-hybrid discovery and immunoprecipitation, with dependence on the ID1 helix-loop-helix domain. The interaction supports a specific signaling complex; downstream Akt activation is not CAV1 kinase catalysis. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18923542 The regulation of the cardiac potassium channel (HERG) by ca... | MODIFY | Summary: Refine hERG association to transmembrane transporter binding. Reason: The complete abstract reports hERG/CAV1 interaction and coimmunoprecipitation, with CAV1-dependent changes in HEK293 hERG current. This supports binding to KCNH2; the channel carries potassium and CAV1 regulates its context. Proposed replacements: transmembrane transporter binding Supporting Evidence: PMID:18923542 HERG channels interact with caveolin-1 |
| GO:0005515 protein binding | IPI PMID:19052258 Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to... | MODIFY | Summary: Refine the channel-complex association to transporter binding. Reason: Selected primary Methods and Results support CAV1 association with TRPC1 and IP3R3 in calcium-entry complexes. CSD deletion weakens association but does not simply abolish all complex formation. These data support the specified channel partner without a purified binary interface or a CAV1 calcium pore. Proposed replacements: transmembrane transporter binding Supporting Evidence: PMID:19052258 effectively interacted with TRPC1 |
| GO:0005515 protein binding | IPI PMID:19052258 Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to... | MODIFY | Summary: Refine the channel-complex association to transporter binding. Reason: Selected primary Methods and Results support CAV1 association with TRPC1 and IP3R3 in calcium-entry complexes. CSD deletion weakens association but does not simply abolish all complex formation. These data support the specified channel partner without a purified binary interface or a CAV1 calcium pore. Proposed replacements: transmembrane transporter binding Supporting Evidence: PMID:19052258 WT-Cav-1 but not Cav-1DeltaCSD interacted with IP(3)R3 |
| GO:0005515 protein binding | IPI PMID:19262564 SRBC/cavin-3 is a caveolin adapter protein that regulates ca... | KEEP AS NON CORE | Summary: CAVIN2 coat association is supported. Reason: The original cavin3-focused abstract does not resolve every CAVIN2 assay. Independent human coat isolation directly coisolates CAVIN2 with CAV1, with GFP/flotillin comparisons. Retain the exact association without asserting a pairwise structural interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19262564 SRBC/cavin-3 is a caveolin adapter protein that regulates ca... | KEEP AS NON CORE | Summary: CAVIN3 association is supported. Reason: The complete source abstract reports CAVIN3 coimmunoprecipitation with CAV1 and dependence on its leucine zipper, with continued association during caveolar vesicle movement. This supports an associated coat component without transferring the partner function wholesale. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19706440 TLR4-mediated expulsion of bacteria from infected bladder ep... | KEEP AS NON CORE | Summary: RAB27B participates in a CAV1-associated exocytic complex. Reason: The complete abstract explicitly places CAV1, RAB27B, PKA and MyRIP in an exocytic complex during bacterial expulsion. This supports coassociation; it is not evidence of GTP hydrolysis or kinase activity by CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19726876 Human PTRF mutations cause secondary deficiency of caveolins... | KEEP AS NON CORE | Summary: CAVIN1 association is independently supported. Reason: The human PTRF mutation abstract reports caveolin association defects, while independent human coat isolation directly coisolates CAVIN1 and CAV1. The disease in the former study is caused by PTRF variants, not evidence of identical CAV1 disease mechanisms. |
| GO:0005515 protein binding | IPI PMID:19820694 Inhibition of thioredoxin reductase 1 by caveolin 1 promotes... | KEEP AS NON CORE | Summary: TXNRD1 binding has specific biochemical support. Reason: The complete abstract reports interaction of the CAV1 scaffolding region with the TXNRD1 binding motif and a binding-deficient enzyme mutant, together with inhibitory effects. Retain this binding context without assigning thioredoxin-reductase chemistry to CAV1; the precise constructs and species were not resolved from a full Methods section. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:19897728 Activation of TRPC1 by STIM1 in ER-PM microdomains involves ... | MODIFY | Summary: Refine the TRPC1 association to transporter binding. Reason: Human salivary-cell experiments support CAV1-dependent surface recruitment of TRPC1 and interaction changes after store depletion. CAV1 overexpression can suppress STIM1-dependent activation despite increased surface channel, so binding does not imply universal activation. Proposed replacements: transmembrane transporter binding Supporting Evidence: PMID:19897728 a decrease in TRPC1-Cav1 clustering |
| GO:0005515 protein binding | IPI PMID:19931615 MLC1 trafficking and membrane expression in astrocytes: role... | KEEP AS NON CORE | Summary: MLC1 association is supported in astrocyte experiments. Reason: The complete abstract reports pull-down of CAV1 by intracellular MLC1 domains and co-fractionation in cultured human and rat astrocytes. The preserved Q15049 partner is MLC1. This does not establish a purified binary interface or transfer all imaged MLC1 compartments to CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20808760 Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake b... | MODIFY | Summary: Refine the PLCG1 interaction to SH2-domain binding. Reason: The recombinant human-domain array identified the PLCG1 SH2 domain as a phospho-Tyr14 CAV1 ligand, and cellular-lysate phosphopeptide pull-down corroborated preferential association. The short array-list anchor names PLCG1 beside VAV2; the selected Results and Fig. 3 caption establish that these are SH2-domain measurements. This is CAV1 binding the partner domain, not CAV1 catalyzing phosphorylation or enabling PLCG1 phospholipase activity. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:20808760 Vav2, Phospholipase CΞ³1 (PLCΞ³1) |
| GO:0005515 protein binding | IPI PMID:20808760 Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake b... | KEEP AS NON CORE | Summary: Retain the exact RASA1 association with an assay-access limit. Reason: The source-specific RASA1 domain-array value was not inspected. The exact P20936-CAV1 interaction is independently present in reviewed UniProt. Retain generic association without copying VAV2 or PLCG1 domain controls onto this partner. Supporting Evidence: UniProt:Q03135 |
| GO:0005515 protein binding | IPI PMID:20808760 Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake b... | MODIFY | Summary: Refine VAV2 association to SH2-domain recognition. Reason: Recombinant human SH2-domain arrays, phospho-Tyr14 peptide pull-down and cellular co-IP support CAV1 recognition by the VAV2 SH2-containing region. Full-length and SH3-SH2-SH3 VAV2 constructs were used in the cellular co-IP; this is not described as a purified single-SH2 pull-down. The exact P52735 partner remains unchanged. CAV1 is the phospholigand, not the guanine-nucleotide exchange factor. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:20808760 high affinity interaction with the SH2 domain of RhoA GEF Vav2 |
| GO:0005515 protein binding | IPI PMID:20808760 Tyrosine-phosphorylated caveolin-1 blocks bacterial uptake b... | MODIFY | Summary: Refine VAV2 association to SH2-domain recognition. Reason: Recombinant human SH2-domain arrays, phospho-Tyr14 peptide pull-down and cellular co-IP support CAV1 recognition by the VAV2 SH2-containing region. Full-length and SH3-SH2-SH3 VAV2 constructs were used in the cellular co-IP; this is not described as a purified single-SH2 pull-down. The exact P52735-1 source product remains unchanged; the assessed array does not independently resolve all isoform-specific differences. Proposed replacements: SH2 domain binding Supporting Evidence: PMID:20808760 Vav2 co-purified exclusively with the phosphorylated peptide |
| GO:0005515 protein binding | IPI PMID:20826780 Factor X/Xa elicits protective signaling responses in endoth... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected official PMC Methods, the complete Fig.5 Results paragraph and caption describe reciprocal anti-PAR1/anti-CAV1 immunoprecipitation in EA.hy926 cells. PAR1 remains associated with CAV1 after FX-S195A while EPCR dissociates; PAR2 provides a distinct nonassociated receptor comparison. This supports a receptor-containing membrane complex, not purified direct binding or a universal protective function. The canonical cache remains abstract-only; the selected body was read through the official indexed PMC result. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20956295 Autophagy protein microtubule-associated protein 1 light cha... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Human Beas-2B coimmunoprecipitation places CAV1 with Fas and LC3B under basal conditions; cigarette-smoke extract disrupts both associations. LC3B Y113A and CAV1 scaffolding-domain deletion reduce the LC3B association, whereas Fas C199S and palmitoylation perturbation affect the Fas association. The study supports specific context-dependent complexes; it does not establish purified binary interfaces or that autophagic flux explains every death effect. Preserve the source Fas isoform identifier without claiming the interaction is unique to that isoform. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:20956295 Autophagy protein microtubule-associated protein 1 light cha... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Human Beas-2B coimmunoprecipitation places CAV1 with Fas and LC3B under basal conditions; cigarette-smoke extract disrupts both associations. LC3B Y113A and CAV1 scaffolding-domain deletion reduce the LC3B association, whereas Fas C199S and palmitoylation perturbation affect the Fas association. The study supports specific context-dependent complexes; it does not establish purified binary interfaces or that autophagic flux explains every death effect. The specific source partner here is MAP1LC3B; Fas is a distinct complex partner and comparison. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected authenticated artifact XML Methods and Results describe human Beas-2B coimmunoprecipitation, primary mouse lung experiments separately, preimmune-IgG controls and time-dependent hyperoxia-associated Fas/CAV1 and BID/CAV1 complexes. CAV1 Y14F impairs BID coassociation and tBID accumulation, whereas WT/Y14D are comparison constructs. These are associations and regulatory perturbations; CAV1 is not the BID-cleaving protease. Canonical source is abstract-only, and the fuller artifact body was consulted without replacing it. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected authenticated artifact XML Methods and Results describe human Beas-2B coimmunoprecipitation, primary mouse lung experiments separately, preimmune-IgG controls and time-dependent hyperoxia-associated Fas/CAV1 and BID/CAV1 complexes. CAV1 Y14F impairs BID coassociation and tBID accumulation, whereas WT/Y14D are comparison constructs. These are associations and regulatory perturbations; CAV1 is not the BID-cleaving protease. Canonical source is abstract-only, and the fuller artifact body was consulted without replacing it. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21822278 Endolysosomal sorting of ubiquitylated caveolin-1 is regulat... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Sequential tagged-VCP isolation followed by native elution and UBXD1 immunoprecipitation coisolates CAV1; endogenous UBXD1 immunoprecipitation supports the specific ternary complex. Disease-associated VCP substitutions and CAV1 ubiquitination perturbations affect the association. The VCP expression construct is rat, human UBXD1 is explicit and human cell systems are used; do not redescribe every construct as human. Both source partners are supported at complex-association level, without assigning direct binary interfaces. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22277751 Caveolin-1 regulates Mcl-1 stability and anoikis in lung car... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Human H460 cells show reciprocal anti-CAV1/anti-MCL1 coimmunoprecipitation, with greater recovery in CAV1-overexpressing cells and lower recovery after CAV1 depletion. Colocalization corroborates the complex. The authors call it direct interaction, but these assays establish coassociation rather than a purified interface. The G361 follow-up supports expression/anoikis regulation, not an independently read reciprocal pull-down in that line. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22411794 Hypoxia promotes ligand-independent EGF receptor signaling v... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The available canonical HTML discussion explicitly reports a hypoxia-associated CAV1/EGFR interaction that diminishes with exogenous ligand and refers to Fig.4C. The actual cache is incomplete for detailed Methods/Results despite its true full-text flag. Exact EGFR association is independently corroborated in the immutable UniProt interaction block; retain a qualified association without asserting that every source control or a direct interface was inspected. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:22614015 The tumour suppressor HACE1 controls cell migration by regul... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The HACE1 paper cache and accessible publisher preview are abstract-only and foreground HACE1/RAC1; they do not establish a citation error. The exact CAV1/RAC1 pair is independently present in the curated UniProt interaction block and supported by the separate PMID:24625804 abstract. Retain qualitative association with explicit original-paper target-assay access limits, without transferring HACE1 ubiquitin-ligase activity to CAV1. |
| GO:0005515 protein binding | IPI PMID:24013648 Molecular composition and ultrastructure of the caveolar coa... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: In human HeLa cells, DSP-stabilized CAV1-GFP coat complexes contain CAV2 and cavins1/2/3 by Western blotting and tandem mass spectrometry; GFP/flotillin2 controls, reciprocal cavin isolations and a mixed-cell control address nonspecific or post-lysis assembly. Human cavin constructs are stated. These are multimeric coat coassociations; the evidence does not establish that each pair contacts directly. Cavin2 abundance is lower in the endogenous coat and can be increased by its tagged overexpression. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24013648 Molecular composition and ultrastructure of the caveolar coa... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: In human HeLa cells, DSP-stabilized CAV1-GFP coat complexes contain CAV2 and cavins1/2/3 by Western blotting and tandem mass spectrometry; GFP/flotillin2 controls, reciprocal cavin isolations and a mixed-cell control address nonspecific or post-lysis assembly. Human cavin constructs are stated. These are multimeric coat coassociations; the evidence does not establish that each pair contacts directly. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24013648 Molecular composition and ultrastructure of the caveolar coa... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: In human HeLa cells, DSP-stabilized CAV1-GFP coat complexes contain CAV2 and cavins1/2/3 by Western blotting and tandem mass spectrometry; GFP/flotillin2 controls, reciprocal cavin isolations and a mixed-cell control address nonspecific or post-lysis assembly. Human cavin constructs are stated. These are multimeric coat coassociations; the evidence does not establish that each pair contacts directly. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24013648 Molecular composition and ultrastructure of the caveolar coa... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: In human HeLa cells, DSP-stabilized CAV1-GFP coat complexes contain CAV2 and cavins1/2/3 by Western blotting and tandem mass spectrometry; GFP/flotillin2 controls, reciprocal cavin isolations and a mixed-cell control address nonspecific or post-lysis assembly. Human cavin constructs are stated. These are multimeric coat coassociations; the evidence does not establish that each pair contacts directly. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The canonical HTML discussion directly reports CAV1/COX2 coimmunoprecipitation and reduced association after COX2 C-terminal deletion or N594A glycosylation-site substitution. Association is not wholly abolished and the precise interface remains unresolved. The cache omits much of Methods/Results, so no complete control audit is claimed. The finding supports an ER degradation-associated complex, not COX catalytic activity by CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:24576892 Caveolin-1 interacts with ATP binding cassette transporter G... | MODIFY | Summary: Refine the generic association to the supported partner class. Reason: The complete PMID:24576892 abstract explicitly reports ABCG1/CAV1 coimmunoprecipitation, flotillin1/2 comparisons, aromatic-residue substitutions affecting association/efflux, and endogenous THP1-derived macrophage observations. These target-specific data support the already present transmembrane-transporter-binding term more informatively than generic binding. Full-body experimental details remain unavailable; do not infer transport catalysis by CAV1 or a purified binding interface. Proposed replacements: transmembrane transporter binding Supporting Evidence: PMID:24576892 ABCG1 co-immunoprecipitated with caveolin-1 (CAV1) |
| GO:0005515 protein binding | IPI PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | MODIFY | Summary: Refine the generic association to the supported partner class. Reason: The complete PMID:24625804 abstract explicitly reports CAV1/RAC1 association during early Salmonella invasion and distinguishes it from formation of Salmonella-containing caveolar vesicles. The exact source partner and reference already support the specific small-GTPase-binding assertion at source row165. Refining this generic assertion to that existing term preserves the function without manufacturing a new process; original full-body details remain unread. Proposed replacements: small GTPase binding Supporting Evidence: PMID:24625804 both proteins colocalized and directly interacted with caveolin-1 |
| GO:0005515 protein binding | IPI PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | UNDECIDED | Summary: The exact source association remains unresolved. Reason: The PMID:24625804 abstract supports RAC1 and SopE but does not resolve the PAK1 source partner. The actual PAK1 pull-down design and whether it functions as an affinity reagent for active RAC1 or as a demonstrated CAV1 partner were not accessible. No exact PAK1 edge appears in the read CAV1 UniProt interaction block. A secondary database search result is a lead, not a substitute for target-specific primary evidence. Preserve the experimental assertion as unresolved rather than removing it or inferring kinase binding. |
| GO:0005515 protein binding | IPI PMID:24658140 The mammalian-membrane two-hybrid assay (MaMTH) for probing ... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The canonical abstract and official publisher preview establish the MaMTH method but the precise CAV1/EGFR assay/table was not accessible. The source IPI assertion and exact curated UniProt EGFR edge, plus the independently read PMID:22411794 CAV1/EGFR discussion, corroborate a qualified association. Do not claim that this exact MaMTH pair was independently revalidated or infer a binary structure from the record. |
| GO:0005515 protein binding | IPI PMID:25285302 The Niemann-Pick C1 and caveolin-1 proteins interact to modu... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Human fibroblast experiments use reciprocal anti-NPC1/anti-CAV1 coimmunoprecipitation under lipoprotein-deficient and LDL-supplemented conditions; the lower molecular-weight NPC1 form preferentially coisolates and association decreases after LDL supplementation. This supports a regulated complex, with explicit glycosylation/condition limits, rather than a demonstrated purified direct interface or a new transport activity for CAV1. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25556234 New host factors important for respiratory syncytial virus (... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The actual canonical body explicitly states that RSV M interacts with all three caveolins and that CAV1 and CAV2 colocalize with M at viral filaments. Thus the CAV1 source pair is supported even though the abstract foregrounds CAV2. Crucially, only CAV2 depletion significantly affected infectivity in the reported comparison; the CAV1 binding row should not imply that phenotype. The accessible body is partial and the full microfluidic assay table was not independently read. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:25588833 Cavin3 interacts with cavin1 and caveolin1 to increase surfa... | UNDECIDED | Summary: The exact source association remains unresolved. Reason: PMID:25588833 explicitly supports cavin3/cavin1/CAV1 organization, but the source combines three partners, including human EHD2. The precise positive EHD2/CAV1 assay, construct identities and all three pair-specific records were not fully resolved. Official publisher/author-PDF access attempts failed. The separate PMID:24013648 study excludes EHD2 from its isolated 80S coat under the tested conditions, which is not universal evidence against other CAV1/EHD2 associations. Preserve all three original partners and the unresolved experimental assertion. |
| GO:0005515 protein binding | IPI PMID:25893292 Syntenin regulates TGF-Ξ²1-induced Smad activation and the ep... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The PMID:25893292 abstract explicitly describes CAV1/TGFBR1 interaction and syntenin-dependent changes in receptor internalization in the studied cancer-cell context. It supports a qualified receptor-associated complex even though syntenin is the paper focus. Full target-assay controls and a direct interface were not accessible, and syntenin effects should not be restated as CAV1 catalytic activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected PMID:31980649 methods distinguish FLAG-bait quantitative AP-MS in HCT116/HKE3 cells from separate membrane yeast-two-hybrid profiling. The exact CAV1/EGFR, CAV1/CAV2 and CAV1/STK38 source pairs are independently present in the immutable UniProt interaction block. Individual supplementary target rows were not inspected, so neither exact assay assignment nor pair-specific replication is claimed. Retain qualified associations without direct-interface, kinase-regulator or universal pathway claims. The exact partner on this assertion is UniProtKB:P00533. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected PMID:31980649 methods distinguish FLAG-bait quantitative AP-MS in HCT116/HKE3 cells from separate membrane yeast-two-hybrid profiling. The exact CAV1/EGFR, CAV1/CAV2 and CAV1/STK38 source pairs are independently present in the immutable UniProt interaction block. Individual supplementary target rows were not inspected, so neither exact assay assignment nor pair-specific replication is claimed. Retain qualified associations without direct-interface, kinase-regulator or universal pathway claims. The exact partner on this assertion is UniProtKB:P51636. |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected PMID:31980649 methods distinguish FLAG-bait quantitative AP-MS in HCT116/HKE3 cells from separate membrane yeast-two-hybrid profiling. The exact CAV1/EGFR, CAV1/CAV2 and CAV1/STK38 source pairs are independently present in the immutable UniProt interaction block. Individual supplementary target rows were not inspected, so neither exact assay assignment nor pair-specific replication is claimed. Retain qualified associations without direct-interface, kinase-regulator or universal pathway claims. The exact partner on this assertion is UniProtKB:Q15208. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The PMID:32814053 abstract describes systematic yeast-two-hybrid screening combined with literature interaction integration; it does not independently resolve these exact rows. UniProt corroborates the exact APP and CSNK1D-2 pairs with CAV1. Preserve the CSNK1D isoform partner and retain qualified source associations, without asserting isoform exclusivity, direct kinase regulation, brain aggregation or a particular screen validation for these pairs. This assertion preserves UniProtKB:P05067. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The PMID:32814053 abstract describes systematic yeast-two-hybrid screening combined with literature interaction integration; it does not independently resolve these exact rows. UniProt corroborates the exact APP and CSNK1D-2 pairs with CAV1. Preserve the CSNK1D isoform partner and retain qualified source associations, without asserting isoform exclusivity, direct kinase regulation, brain aggregation or a particular screen validation for these pairs. This assertion preserves UniProtKB:P48730-2. |
| GO:0005515 protein binding | IPI PMID:33845483 Multilevel proteomics reveals host perturbations by SARS-CoV... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: The canonical PMID:33845483 abstract describes multilevel viral-host proteomics in a lung-derived human cell line, but the exact processed viral partner table was not read. The identical PRO_0000449624 partner is present in the CAV1 UniProt interaction block and recurs in independent source records. Retain a qualified xenoprotein association, preserving the processed-product ID and avoiding an unverified assay, viral stage or host physiological function. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected authenticated BioPlex XML methods establish affinity-tagged bait expression and anti-HA purification in 293T/HCT116 cells, while discussing incomplete reproducibility and direct versus indirect complex edges. The exact CAV1/CAV2 pair is independently corroborated by UniProt and the primary coat-complex experiments. The specific BioPlex target table and per-pair replication were not read; retain the qualified association without assigning those network-wide rates to this pair. |
| GO:0005515 protein binding | IPI PMID:34232536 Interactomes of SARS-CoV-2 and human coronaviruses reveal ho... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected authenticated PMID:34232536 XML methods distinguish SFB tandem affinity purification from BioID2 proximity labeling in human cells, with tag/vector/GFP controls, triplicates and SAINT filtering. The exact processed viral partner is independently corroborated in UniProt. Its individual supplementary assay provenance remains unread, so retain only qualified association and do not equate proximity or co-complex membership with purified direct binding. |
| GO:0005515 protein binding | IPI PMID:36217030 A comprehensive SARS-CoV-2-human protein-protein interactome... | KEEP AS NON CORE | Summary: Retain the supported association as non-core. Reason: Selected authenticated PMID:36217030 XML methods distinguish Y2H binary screens from tagged-bait AP-MS co-complex assays in Caco2 cells, with matched empty vectors and biological duplicates. Exact per-pair assay assignment was not read. The preserved processed viral partner is corroborated by UniProt and independent source records; retain qualified association without claiming that this pair was positive in both assay classes or assigning an untested infection mechanism. |
| GO:0005737 cytoplasm | IDA PMID:26918609 c-Src/Cav1-dependent activation of the EGFR by Dsg2. | KEEP AS NON CORE | Summary: Intracellular CAV1 redistribution supports broad cytoplasmic localization. Reason: The actual Dsg2 study uses human HaCaT keratinocytes. Selected Results and Fig. 8 caption describe CAV1 at cell borders and redistribution into the intracellular region with Dsg2 expression. This supports broad cytoplasm, which includes membrane-associated structures; it does not establish freely soluble CAV1. Supporting Evidence: PMID:26918609 higher Dsg2 expression redistributed Cav1 intracellularly |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Broad cytoplasm is a compatible, nonspecific localization. Reason: GO_REF:0000044 maps a UniProt subcellular-location vocabulary term. Intracellular membrane and vesicular pools support the broad location; a soluble cytosolic role is not inferred. Supporting Evidence: UniProt:Q03135 |
| GO:0005768 endosome | IDA PMID:20682791 A protein interaction network for Ecm29 links the 26 S prote... | KEEP AS NON CORE | Summary: Retain the caveolin-marked endosomal compartment. Reason: The actual Ecm29 study describes caveolin-decorated endosomes as a comparison population largely lacking Ecm29-proteasome complexes. The positive CAV1 location is retained without transferring Ecm29 adaptor activity or describing this as the separate VCP-dependent CAV1 degradation study. Supporting Evidence: |
| GO:0005783 endoplasmic reticulum | IDA PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | KEEP AS NON CORE | Summary: ER localization is retained with experimental curator deference. Reason: The primary BENE abstract does not expose every compartment-marker panel. Its CAV1 trafficking observations and independent ER-associated degradation evidence support retention of the annotated ER pool, without claiming the original ER image was inspected. |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The ER pool is consistent with CAV1 synthesis and trafficking. Reason: The mouse ortholog transfer agrees with human ER-associated CAV1 interactions. This broad compartment is retained; the specific mouse localization experiment has not been re-read. Supporting Evidence: |
| GO:0005789 endoplasmic reticulum membrane | TAS PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: CAV1 acts in an ER-associated protein-degradation context. Reason: The complete available Discussion describes CAV1 association with Derlin-1, p97 and COX-2 during retrotranslocation. The canonical HTML extraction omits the Results and Methods, so exact topology and construct controls are not claimed. Supporting Evidence: |
| GO:0005794 Golgi apparatus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Golgi residence is a conserved trafficking context. Reason: The PAINT assertion agrees with the reviewed CAV1 Golgi pool. The target appearing among descendant evidence is legitimate; the actual ancestral placement was not inspected and is not declared circular. Supporting Evidence: UniProt:Q03135 |
| GO:0005794 Golgi apparatus | IDA GO_REF:0000052 | KEEP AS NON CORE | Summary: Retain the immunofluorescence-supported Golgi pool. Reason: GO_REF:0000052 identifies an immunofluorescence localization method, rather than a gene-mechanism paper. The exact original image is uninspected, but the localization is consistent with the reviewed CAV1 record. Supporting Evidence: UniProt:Q03135 |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: Retain the Golgi localization supported by combined electronic sources. Reason: The combined UniProt-location and ortholog evidence is biologically consistent with CAV1 trafficking. This does not independently validate each underlying prediction rule. Supporting Evidence: UniProt:Q03135 |
| GO:0005811 lipid droplet | TAS Reactome:R-HSA-202144 | UNDECIDED | Summary: The lipid-droplet location of this particular reaction-associated pool is unresolved. Reason: The complete cached Reactome summaries describe CAV1-eNOS association or dissociation but do not establish the lipid-droplet compartment assigned to these two assertions. CAV1 can have intracellular lipid-associated pools, so a source-specific compartment audit is needed rather than a blanket localization rejection. |
| GO:0005811 lipid droplet | TAS Reactome:R-HSA-203712 | UNDECIDED | Summary: The lipid-droplet location of this particular reaction-associated pool is unresolved. Reason: The complete cached Reactome summaries describe CAV1-eNOS association or dissociation but do not establish the lipid-droplet compartment assigned to these two assertions. CAV1 can have intracellular lipid-associated pools, so a source-specific compartment audit is needed rather than a blanket localization rejection. |
| GO:0005886 plasma membrane | IDA GO_REF:0000054 | ACCEPT | Summary: Plasma-membrane localization is central to CAV1 function. Reason: The source method is live-cell imaging of a fusion protein. The exact source image is not re-inspected, but direct caveolar imaging and coat isolation independently establish this location. Supporting Evidence: PMID:24013648 caveolin-1-GFP, localised around the caveolar bulb |
| GO:0005886 plasma membrane | IDA PMID:23262137 The myosin motor Myo1c is required for VEGFR2 delivery to th... | ACCEPT | Summary: CAV1 is present in plasma-membrane domains. Reason: The experimental localization is consistent with the raft and caveolar pool described in this source and independently resolved by caveolar coat imaging. No universal equivalence of every raft with a caveola is implied. Supporting Evidence: PMID:23262137 recruitment of VEGFR2 to the PM and its colocalization with Myo1c and caveolin-1 |
| GO:0005886 plasma membrane | IDA PMID:26918609 c-Src/Cav1-dependent activation of the EGFR by Dsg2. | ACCEPT | Summary: Retain the plasma-membrane fluorescence annotation. Reason: The actual Dsg2 study reports CAV1 cell-border staining and membrane fractionation in human HaCaT keratinocytes. Selected Results and Fig. 8 caption independently support the membrane pool; original image pixels were not reanalyzed. |
| GO:0005886 plasma membrane | IEA GO_REF:0000120 | ACCEPT | Summary: Electronic plasma-membrane localization agrees with direct evidence. Reason: The combined mouse ortholog and UniProt-location mapping agrees with the physical CAV1 caveolar membrane pool. Supporting Evidence: |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202110 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202129 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-202144 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-203565 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-203625 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-203662 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-203712 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-203716 | ACCEPT | Summary: Retain the plasma-membrane CAV1 pool in eNOS-associated reactions. Reason: The complete Reactome summaries place CAV1 in membrane-associated eNOS binding, release or trafficking events. The location is independently supported; the activity of eNOS, calmodulin, HSP90, NOSTRIN or dynamin is not transferred to CAV1. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-209815 | ACCEPT | Summary: Retain membrane residence in the curated thyroid-hormone reaction context. Reason: The curated thyroxisome events include CAV1 as a membrane-associated organizer. They do not establish peroxidase, oxidase or hormone-synthetic chemistry by CAV1. The plasma-membrane location itself is well supported. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-209840 | ACCEPT | Summary: Retain membrane residence in the curated thyroid-hormone reaction context. Reason: The curated thyroxisome events include CAV1 as a membrane-associated organizer. They do not establish peroxidase, oxidase or hormone-synthetic chemistry by CAV1. The plasma-membrane location itself is well supported. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-209925 | ACCEPT | Summary: Retain membrane residence in the curated thyroid-hormone reaction context. Reason: The curated thyroxisome events include CAV1 as a membrane-associated organizer. They do not establish peroxidase, oxidase or hormone-synthetic chemistry by CAV1. The plasma-membrane location itself is well supported. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-209973 | ACCEPT | Summary: Retain membrane residence in the curated thyroid-hormone reaction context. Reason: The curated thyroxisome events include CAV1 as a membrane-associated organizer. They do not establish peroxidase, oxidase or hormone-synthetic chemistry by CAV1. The plasma-membrane location itself is well supported. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-350901 | ACCEPT | Summary: Retain membrane residence in the curated thyroid-hormone reaction context. Reason: The curated thyroxisome events include CAV1 as a membrane-associated organizer. They do not establish peroxidase, oxidase or hormone-synthetic chemistry by CAV1. The plasma-membrane location itself is well supported. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5368596 | ACCEPT | Summary: Retain CAV1 plasma-membrane residence during receptor uptake. Reason: The curated WNT3A-LRP6 internalization event agrees with the independently supported membrane-associated CAV1 pool. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-5693681 | ACCEPT | Summary: Retain membrane residence in the curated thyroid-hormone reaction context. Reason: The curated thyroxisome events include CAV1 as a membrane-associated organizer. They do not establish peroxidase, oxidase or hormone-synthetic chemistry by CAV1. The plasma-membrane location itself is well supported. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9013145 | ACCEPT | Summary: Retain the membrane CAV1 pool in small-GTPase regulation. Reason: The curated RAC1/CDC42 contexts locate CAV1 at membranes. Their descriptions do not make CAV1 a GTPase or transfer a partner catalytic activity. Supporting Evidence: Reactome:R-HSA-9013145 Reactome:R-HSA-9013158 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9013158 | ACCEPT | Summary: Retain the membrane CAV1 pool in small-GTPase regulation. Reason: The curated RAC1/CDC42 contexts locate CAV1 at membranes. Their descriptions do not make CAV1 a GTPase or transfer a partner catalytic activity. Supporting Evidence: Reactome:R-HSA-9013145 Reactome:R-HSA-9013158 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9021079 | ACCEPT | Summary: Retain the destination membrane pool in estrogen-receptor trafficking. Reason: The complete event describes CAV1-associated estrogen receptor arriving at the plasma membrane. This is localization evidence, not a CAV1 steroid-receptor activity. Supporting Evidence: Reactome:R-HSA-9021079 |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-9624985 | ACCEPT | Summary: The plasma-membrane location is independently established. Reason: The Reactome event concerns regulation of CAV1 expression and is not itself a localization experiment. The source annotation is retained because the membrane pool is directly established elsewhere, without attributing FOXO transcription-factor activity to CAV1. Supporting Evidence: |
| GO:0005901 caveola | IBA GO_REF:0000033 | ACCEPT | Summary: Caveolar localization is a conserved defining property. Reason: Direct human coat isolation and localization support the PAINT term. Caveolin paralogs in the donor set do not by themselves invalidate the ancestral assertion; the actual PTN placement was not inspected. Supporting Evidence: |
| GO:0005901 caveola | IDA PMID:15219854 N-terminal processing and modifications of caveolin-1 in cav... | ACCEPT | Summary: Retain the experimental caveolar localization. Reason: The cited study is consistent with the defining caveolar CAV1 pool, independently demonstrated in human coat preparations. The exact original microscopy panel is uninspected. Supporting Evidence: PMID:15219854 caveolae vesicles isolated from primary human adipocytes |
| GO:0005901 caveola | IDA PMID:15703204 Maxi-K channels localize to caveolae in human myometrium: a ... | ACCEPT | Summary: Human myometrial CAV1 is present in caveolar channel complexes. Reason: The complete abstract describes caveolar fractionation, colocalization and immunoelectron microscopy in human myometrium and derived cells. Channel conductance belongs to the maxi-K channel rather than CAV1. Supporting Evidence: PMID:15703204 colocalization of maxi-K channels, actin, and caveolin-1 |
| GO:0005901 caveola | IDA PMID:17982011 Caveolin-1 and caveolin-3 form heterooligomeric complexes in... | ACCEPT | Summary: Retain caveolar localization in the cardiac study. Reason: The complete abstract explicitly reports mouse and rat atrial myocytes, heterooligomeric CAV1/CAV3 complexes and knockout-mouse apoptosis experiments. Retain the curated localization with independent human CAV1 caveolar evidence, without redescribing the original cells as human or treating the CAV3 partner as a CAV1 isoform. Supporting Evidence: PMID:17982011 caveolin-1 and caveolin-3 can interact and form heterooligomeric complexes |
| GO:0005901 caveola | IDA PMID:18081315 Serine 23 and 36 phosphorylation of caveolin-2 is differenti... | ACCEPT | Summary: Retain the experimental caveolar CAV1 pool. Reason: The source is compatible with CAV1 caveolar localization, independently established by direct human imaging. The original source-specific microscopy and construct controls were not all accessible. Supporting Evidence: PMID:18081315 caveolin-1-driven targeting to plasma membrane lipid rafts and caveolae |
| GO:0005901 caveola | IDA PMID:19525939 SDPR induces membrane curvature and functions in the formati... | ACCEPT | Summary: CAV1 localization accompanies caveolar coat assembly. Reason: The available source describes cavin-dependent caveolar organization. This is consistent with CAV1 as a membrane coat component rather than evidence that CAV1 and every cavin have interchangeable functions. Supporting Evidence: PMID:19525939 STB colocalizes extensively with both SDPR and caveolin 1 |
| GO:0005901 caveola | IDA PMID:24013648 Molecular composition and ultrastructure of the caveolar coa... | ACCEPT | Summary: CAV1 is a physical component of the caveolar coat. Reason: Selected human HeLa biochemical isolation and immuno-EM Results show endogenous and tagged CAV1 around caveolar bulbs. Cross-linking stabilizes an otherwise detergent-sensitive coat; neither a universal native stoichiometry nor direct EHD2 contact is inferred. Supporting Evidence: PMID:24013648 caveolin-1-GFP, localised around the caveolar bulb |
| GO:0005901 caveola | IDA PMID:25556234 New host factors important for respiratory syncytial virus (... | ACCEPT | Summary: Retain the caveolar localization despite the CAV2-focused viral context. Reason: CAV1 is a relevant caveolar marker and the annotated location is independently established. Distinct CAV1 and CAV2 viral-phenotype effects do not negate CAV1 localization. |
| GO:0005901 caveola | IEA GO_REF:0000120 | ACCEPT | Summary: The electronic caveolar location agrees with direct evidence. Reason: The combined ortholog, ARBA and UniProt-location sources converge on a defining CAV1 compartment. Individual ARBA feature logic was not inspected. Supporting Evidence: |
| GO:0005925 focal adhesion | HDA PMID:21423176 Analysis of the myosin-II-responsive focal adhesion proteome... | KEEP AS NON CORE | Summary: Retain focal-adhesion association as a non-core localization. Reason: The exact CAV1 proteomic table entry was not re-read, but independent CAV1 focal-adhesion localization supports the curated HDA assignment. This does not imply CAV1 is an integrin or a focal-adhesion kinase. |
| GO:0005925 focal adhesion | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the inherited focal-adhesion context. Reason: Human CAV1 has independent focal-adhesion evidence. Mixed caveolin descendant evidence does not establish a PAINT error; the ancestral placement and alignment remain uninspected. |
| GO:0005925 focal adhesion | IDA PMID:12091389 Src-induced phosphorylation of caveolin-2 on tyrosine 19. Ph... | KEEP AS NON CORE | Summary: Focal-adhesion CAV1 is a supported context-dependent pool. Reason: The annotated imaging result is consistent with phosphorylation-dependent CAV1 localization at focal adhesions. It is retained without assuming all caveolae are focal adhesions. |
| GO:0005925 focal adhesion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: The focal-adhesion transfer has independent human support. Reason: The mouse donor mapping is retained because the corresponding human CAV1 localization is supported independently. This does not constitute reinspection of the donor experiment. |
| GO:0005929 cilium | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific ciliary localization transfer remains unresolved. Reason: The donor graph provides a mouse localization precedent, but the actual cell type, ciliary marker and CAV1 compartment controls have not been inspected. A generic membrane protein can occur in cilia, so no taxonomic or paralog-based rejection is warranted. |
| GO:0005938 cell cortex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 association with the membrane-proximal cortex is plausible and supported. Reason: Human CAV1 is recruited to membrane-associated actin structures in the bacterial-attachment experiments. Retain this broad cortex transfer while distinguishing membrane-associated organization from an actin structural-subunit activity. Supporting Evidence: |
| GO:0006641 triglyceride metabolic process | ISS GO_REF:0000024 | UNDECIDED | Summary: The specific triglyceride-metabolism transfer requires its donor assay. Reason: The mouse transfer concerns chemical transformations involving triglycerides. This differs from the broader accumulation and maintenance endpoint of lipid storage. Human CAV1 loss and adipocyte membrane defects corroborate storage capacity, but do not identify the target chemical step or distinguish direct metabolic regulation from secondary changes in substrate access or tissue organization. The exact mouse donor experiment for this assertion was not resolved, so retain UNDECIDED rather than infer a specific triglyceride-metabolism mechanism from lipodystrophy. |
| GO:0006816 calcium ion transport | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain a calcium-handling role through organization of channel complexes. Reason: CAV1 changes TRPC1 surface retention and its association with IP3 receptors and STIM1. This supports calcium handling, while the channel performs ion conduction. Effects vary with partner abundance and activation state. |
| GO:0006874 intracellular calcium ion homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain a calcium-handling role through organization of channel complexes. Reason: CAV1 changes TRPC1 surface retention and its association with IP3 receptors and STIM1. This supports calcium handling, while the channel performs ion conduction. Effects vary with partner abundance and activation state. |
| GO:0006940 regulation of smooth muscle contraction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Smooth-muscle contraction regulation is a downstream physiological context. Reason: The human myometrial channel-complex study supports a link between caveolar organization and potassium-current regulation. Retain the mouse-derived regulatory context without assigning myosin motor activity or channel conductance to CAV1. Supporting Evidence: |
| GO:0007519 skeletal muscle tissue development | ISS GO_REF:0000024 | UNDECIDED | Summary: The particular skeletal-muscle developmental role remains unresolved. Reason: The source specifies mouse Cav1, not Cav3. A CAV3 role is not evidence of misattribution, but the actual Cav1 donor experiment and relevant cellular compartment were not inspected. |
| GO:0008104 intracellular protein localization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: CAV1 organizes intracellular localization of selected proteins. Reason: TRPC1 surface-retention and caveolar trafficking experiments support this broad localization role. It does not imply that CAV1 transports every partner or catalyzes vesicle movement. |
| GO:0008142 oxysterol binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the curated oxysterol-binding assignment with bounded provenance. Reason: The reviewed UniProt record reports oxysterol binding by similarity, consistent with the specified mouse ortholog. Exact ligand-specific affinity and construct controls were not re-read, so this remains a retained non-core binding context rather than a new sterol-receptor mechanism. Supporting Evidence: UniProt:Q03135 |
| GO:0008142 oxysterol binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the curated oxysterol-binding assignment with bounded provenance. Reason: The reviewed UniProt record reports oxysterol binding by similarity, consistent with the specified mouse ortholog. Exact ligand-specific affinity and construct controls were not re-read, so this remains a retained non-core binding context rather than a new sterol-receptor mechanism. Supporting Evidence: UniProt:Q03135 |
| GO:0009617 response to bacterium | IDA PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | KEEP AS NON CORE | Summary: Bacterial exposure engages CAV1-dependent membrane signaling. Reason: The primary abstract links CAV1, RAC1 and membrane ruffling to bacterial uptake. This is a defined host-cell response, not a general antimicrobial enzyme function. Supporting Evidence: |
| GO:0010524 positive regulation of calcium ion transport into cytosol | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 can promote calcium entry in the tested scaffold context. Reason: The TRPC1 study compares CAV1-null endothelial cells and rescue constructs. Wild-type CAV1 restores entry, but a scaffolding-domain deletion can further increase current despite weaker association. Retain the directional context without making CAV1 a universal calcium-channel activator. Supporting Evidence: |
| GO:0010524 positive regulation of calcium ion transport into cytosol | ISS PMID:19052258 Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to... | KEEP AS NON CORE | Summary: CAV1 can promote calcium entry in the tested scaffold context. Reason: The TRPC1 study compares CAV1-null endothelial cells and rescue constructs. Wild-type CAV1 restores entry, but a scaffolding-domain deletion can further increase current despite weaker association. Retain the directional context without making CAV1 a universal calcium-channel activator. Supporting Evidence: PMID:19052258 gain-of-function in Ca(2+) entry |
| GO:0010608 post-transcriptional regulation of gene expression | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Post-transcriptional regulation is supported as a partner-specific consequence. Reason: In human H460 and G361 cells, CAV1 changes MCL1 ubiquitination and protein stability after detachment. This supports a broad post-transcriptional role without assigning ubiquitin-ligase or deubiquitinase catalysis to CAV1. Supporting Evidence: |
| GO:0010628 positive regulation of gene expression | IEA GO_REF:0000107 | UNDECIDED | Summary: The exact positive gene-expression transfer remains unresolved. Reason: A signaling scaffold can alter gene expression in multiple directions. The particular mouse donor experiment, gene target and causal regulatory endpoint were not accessed, so no universal positive-expression role is asserted. |
| GO:0010875 positive regulation of cholesterol efflux | IDA PMID:24576892 Caveolin-1 interacts with ATP binding cassette transporter G... | KEEP AS NON CORE | Summary: CAV1 promotes cholesterol efflux in a transporter-dependent context. Reason: The source reports CAV1 association with ABCG1 and effects on cholesterol efflux. ABCG1 supplies transporter activity; CAV1 is a regulator or organizer rather than an ATP-driven cholesterol pump. Supporting Evidence: |
| GO:0015485 cholesterol binding | TAS PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | KEEP AS NON CORE | Summary: Retain cholesterol binding with the stated source limitation. Reason: The cited BENE abstract principally supports raft trafficking, not a stand-alone affinity measurement. The reviewed CAV1 sterol-associated membrane role supports retention of the curator assertion; no binding constant or exact binding-site mechanism is claimed. |
| GO:0016020 membrane | IDA PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | ACCEPT | Summary: Membrane association is integral to CAV1 function. Reason: Membrane recruitment and caveolar localization are directly supported. This broad location is retained without equating every CAV1 membrane pool with a morphologically defined caveola. Supporting Evidence: PMID:24625804 caveolae rapidly moved to the apical plasma membrane |
| GO:0016020 membrane | IEA GO_REF:0000107 | ACCEPT | Summary: Membrane association is integral to CAV1 function. Reason: Membrane recruitment and caveolar localization are directly supported. This broad location is retained without equating every CAV1 membrane pool with a morphologically defined caveola. |
| GO:0016050 vesicle organization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Broad vesicle organization is retained as a non-core trafficking context. Reason: The canine ortholog transfer is compatible with human caveolar coat organization and the experimentally characterized CAV1-associated trafficking pool. GO:0016050 covers assembly, arrangement or disassembly of vesicles broadly. Retain this umbrella assertion with curator deference as a non-core context; the structural core is stated more precisely as CAV1 coat scaffolding in caveola assembly. The exact canine donor assay is uninspected, and neither generic vesicle fusion nor CAV1 acting alone in scission is inferred. |
| GO:0016504 peptidase activator activity | IEA GO_REF:0000107 | UNDECIDED | Summary: Direct peptidase activation is not yet resolved from the donor evidence. Reason: The specified mouse ortholog transfer requires distinguishing local retention of protease in membrane domains from direct enhancement of protease catalytic activity. The traced donor evidence reports different effects in whole-heart and raft fractions and peptide-mediated inhibition. Without the full donor activity and localization controls, neither an unqualified activator assignment nor its reversal is justified. Protease association or altered local abundance is not itself an assay of CAV1 increasing protease catalytic activity. The unread donor controls also prevent a confident over-annotation verdict; this uncertainty is not converted into a negative activity claim. |
| GO:0016504 peptidase activator activity | ISS GO_REF:0000024 | UNDECIDED | Summary: Direct peptidase activation is not yet resolved from the donor evidence. Reason: The specified mouse ortholog transfer requires distinguishing local retention of protease in membrane domains from direct enhancement of protease catalytic activity. The traced donor evidence reports different effects in whole-heart and raft fractions and peptide-mediated inhibition. Without the full donor activity and localization controls, neither an unqualified activator assignment nor its reversal is justified. Protease association or altered local abundance is not itself an assay of CAV1 increasing protease catalytic activity. The unread donor controls also prevent a confident over-annotation verdict; this uncertainty is not converted into a negative activity claim. |
| GO:0019065 receptor-mediated endocytosis of virus by host cell | IGI PMID:21047970 The Tyro3 receptor kinase Axl enhances macropinocytosis of Z... | KEEP AS NON CORE | Summary: Retain the experimentally curated viral-entry context. Reason: The cited genetic-interaction experiment tests a receptor-mediated entry route. A requirement for caveolar organization is compatible with CAV1 participation in that route, without making CAV1 the viral receptor or generalizing to all viruses. Supporting Evidence: |
| GO:0019217 regulation of fatty acid metabolic process | ISS GO_REF:0000024 | UNDECIDED | Summary: The particular fatty-acid-metabolism regulatory endpoint is unresolved. Reason: This mouse transfer asserts modulation of fatty-acid chemical metabolism, beyond accumulation or maintenance of lipid reserves. The precise donor experiment and regulatory endpoint remain uninspected. Human lipodystrophy and altered membrane lipid handling corroborate a storage-related physiological role but do not settle this distinct metabolic-regulation assertion or establish a direction. Retain UNDECIDED without implying that metabolism can never depend on CAV1. |
| GO:0019899 enzyme binding | IPI PMID:20122998 The role of prostacyclin synthase and thromboxane synthase s... | UNDECIDED | Summary: The particular enzyme-binding assay remains unverified. Reason: The cited source is a review whose complete abstract does not expose the specific CAV1βQ16647 prostacyclin-synthase interaction. The underlying target assay was not recovered and no independent exact-edge corroboration was established here. Preserve the experimental source object as unresolved rather than infer enzyme binding from a general cancer-signaling discussion. Supporting Evidence: |
| GO:0019901 protein kinase binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Protein kinase binding is supported independently of the PAINT placement. Reason: Human CAV1-Src coassociation is directly supported. The target as descendant evidence is legitimate and the ancestral placement is uninspected; binding does not make CAV1 a kinase. Supporting Evidence: |
| GO:0019901 protein kinase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 associates with Src-family kinase machinery. Reason: Human CAV1-GFP coimmunoprecipitation supports Src association. CAV1 is also a phosphorylated substrate and regulator; neither binding nor phosphorylation confers kinase catalysis. Supporting Evidence: |
| GO:0019901 protein kinase binding | IPI PMID:25006397 Nitrosation-dependent caveolin 1 phosphorylation, ubiquitina... | KEEP AS NON CORE | Summary: CAV1 associates with Src-family kinase machinery. Reason: Human CAV1-GFP coimmunoprecipitation supports Src association. CAV1 is also a phosphorylated substrate and regulator; neither binding nor phosphorylation confers kinase catalysis. Supporting Evidence: |
| GO:0019915 lipid storage | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Lipid storage is retained as a broad, non-core physiological context. Reason: GO:0019915 concerns accumulation and maintenance of lipids in cells or tissues, rather than a particular chemical transformation. Retain the curated mouse ortholog transfer at that broad contextual level: human CAV1 deficiency causes loss of normal adipose storage, and direct human adipocyte caveolar preparations independently place CAV1 in the relevant membrane architecture. These observations corroborate physiological relevance, not a newly demonstrated lipid-synthetic activity or a re-read of the original mouse donor assay. They therefore support non-core retention of the existing storage assertion without resolving the separate triglyceride-metabolism and fatty-acid-metabolism-regulation endpoints. |
| GO:0030154 cell differentiation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Differentiation is a broad inherited contextual role. Reason: The PAINT assertion is retained as a pleiotropic outcome of caveolin-dependent membrane organization and signaling. The actual ancestral placement is uninspected; donor diversity alone is not a failure argument. |
| GO:0030193 regulation of blood coagulation | IMP PMID:17848177 Tissue factor induction by protease-activated receptor 1 req... | KEEP AS NON CORE | Summary: Coagulation regulation is a context of thrombomodulin/PAR signaling. Reason: The complete structured abstract reports human endothelial PAR1βCAV1 coimmunoprecipitation, cholesterol-dependent compartmentalization and reduced PAR1-induced tissue-factor activation after CAV1 siRNA. This supports a contextual procoagulant regulatory role; it does not assign tissue-factor or thrombin activity to CAV1. Supporting Evidence: PMID:17848177 siRNA directed against caveolin-1 inhibited TF activation |
| GO:0030292 protein tyrosine kinase inhibitor activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 can restrain Src activation in cells. Reason: Selected human CAV1-GFP experiments connect CAV1-Src association with reduced activating-site phosphorylation. C156S also disrupts oligomerization and localization, so the mutation is not a clean binding-only test. The activity is retained as cellular regulation, not purified Src inhibition kinetics. Supporting Evidence: |
| GO:0030292 protein tyrosine kinase inhibitor activity | IMP PMID:25006397 Nitrosation-dependent caveolin 1 phosphorylation, ubiquitina... | KEEP AS NON CORE | Summary: CAV1 can restrain Src activation in cells. Reason: Selected human CAV1-GFP experiments connect CAV1-Src association with reduced activating-site phosphorylation. C156S also disrupts oligomerization and localization, so the mutation is not a clean binding-only test. The activity is retained as cellular regulation, not purified Src inhibition kinetics. Supporting Evidence: |
| GO:0030292 protein tyrosine kinase inhibitor activity | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: CAV1 can restrain Src activation in cells. Reason: Selected human CAV1-GFP experiments connect CAV1-Src association with reduced activating-site phosphorylation. C156S also disrupts oligomerization and localization, so the mutation is not a clean binding-only test. The activity is retained as cellular regulation, not purified Src inhibition kinetics. Supporting Evidence: |
| GO:0030301 cholesterol transport | TAS PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | KEEP AS NON CORE | Summary: Cholesterol trafficking is a supported membrane-associated role. Reason: The cited BENE study follows CAV1-associated redistribution after cholesterol oxidation and recovery. Retain trafficking participation while distinguishing organization of sterol-rich domains from an active cholesterol-transporter mechanism. Supporting Evidence: |
| GO:0030335 positive regulation of cell migration | IMP PMID:21109942 Caveolin-1 mediates tumor cell migration and invasion and it... | KEEP AS NON CORE | Summary: Positive migration regulation is a context-dependent phenotype. Reason: The cited perturbation study supports a migration endpoint. It is retained as a non-core signaling consequence, not as a motor activity or a universal direction of CAV1 effects on migration. Supporting Evidence: |
| GO:0030666 endocytic vesicle membrane | TAS Reactome:R-HSA-203625 | KEEP AS NON CORE | Summary: CAV1 can reside on internalized caveolar membrane. Reason: The complete Reactome event describes redistribution of the CAV1-eNOS complex with NOSTRIN during endocytosis. The vesicle-membrane localization is compatible with CAV1 trafficking. Supporting Evidence: Reactome:R-HSA-203625 |
| GO:0030674 protein-macromolecule adaptor activity | IEA GO_REF:0000107 | ACCEPT | Summary: CAV1 organizes protein and membrane-associated signaling assemblies. Reason: Human TRPC1 surface retention, its recruitment into STIM1-associated domains and coordinated channel-complex association support an adaptor contribution. This partner-organization activity is distinct from the integral structural scaffolding of the caveolin oligomer; neither channel conduction nor partner catalytic activity is assigned to CAV1. |
| GO:0030857 negative regulation of epithelial cell differentiation | ISS GO_REF:0000024 | UNDECIDED | Summary: The exact epithelial differentiation repression transfer is unresolved. Reason: The mouse developmental model and causal differentiation endpoint were not inspected. A role in membrane signaling does not by itself determine this specific direction or tissue context. |
| GO:0030879 mammary gland development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the mouse-derived mammary developmental role. Reason: The cached primary abstract reports accelerated lobuloalveolar development and premature milk production in female Cav1-null mice. Selected external Results link the phenotype to prolactin/JAK2/STAT5 signaling. Retain the original mouse-derived developmental context as non-core without claiming a direct human mammary-development experiment. Supporting Evidence: |
| GO:0031267 small GTPase binding | IPI PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | KEEP AS NON CORE | Summary: RAC1 association supports the specific small-GTPase binding term. Reason: The primary report links CAV1-RAC1 interaction and membrane ruffling in bacterial entry. CAV1 is not thereby assigned intrinsic GTP hydrolysis or guanine-nucleotide exchange activity. Supporting Evidence: |
| GO:0031295 T cell costimulation | IDA PMID:17287217 Caveolin-1 triggers T-cell activation via CD26 in associatio... | KEEP AS NON CORE | Summary: Retain the CD26-dependent T-cell costimulation context. Reason: The source describes CAV1 binding to CD26 on activated T cells and an antigen-presenting-cell signaling response. This is context-specific costimulation, not a T-cell receptor ligand identity or autonomous transcription activity. Supporting Evidence: |
| GO:0031397 negative regulation of protein ubiquitination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 reduces MCL1 ubiquitination in detached cancer cells. Reason: The human H460/G361 experiments combine CAV1 expression perturbation, MCL1 immunoprecipitation and ubiquitin detection. They support a partner-specific stabilizing effect; the precise steric mechanism remains proposed and no deubiquitinase catalysis is inferred. Supporting Evidence: |
| GO:0031397 negative regulation of protein ubiquitination | IMP PMID:22277751 Caveolin-1 regulates Mcl-1 stability and anoikis in lung car... | KEEP AS NON CORE | Summary: CAV1 reduces MCL1 ubiquitination in detached cancer cells. Reason: The human H460/G361 experiments combine CAV1 expression perturbation, MCL1 immunoprecipitation and ubiquitin detection. They support a partner-specific stabilizing effect; the precise steric mechanism remains proposed and no deubiquitinase catalysis is inferred. Supporting Evidence: |
| GO:0031398 positive regulation of protein ubiquitination | IMP PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: CAV1 promotes COX2 ubiquitination within an ERAD assembly. Reason: The available complete Discussion describes enhanced association of COX2, Derlin-1, p97 and Ufd1. Retain the experimental regulatory assertion while acknowledging that this HTML cache omits the original Results/Methods. CAV1 is not assigned ubiquitin-ligase chemistry. Supporting Evidence: |
| GO:0031410 cytoplasmic vesicle | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cytoplasmic vesicles are a conserved trafficking compartment. Reason: The PAINT location agrees with direct CAV1 endocytic-trafficking evidence. The node placement was not inspected, and the target descendant does not constitute circular support. Supporting Evidence: |
| GO:0031410 cytoplasmic vesicle | IDA PMID:19931615 MLC1 trafficking and membrane expression in astrocytes: role... | KEEP AS NON CORE | Summary: Retain the intracellular vesicle pool in the MLC1 trafficking study. Reason: The complete MLC1 abstract reports human and rat astrocyte pull-down/cofractionation with CAV1 and MLC1 vesicular trafficking. Its localization prose foregrounds MLC1, so the original CAV1 compartment-marker panels remain uninspected. Retain the broad CAV1 vesicle annotation with curator deference and independently supported CAV1 trafficking, without substituting PACSIN2 for MLC1. Supporting Evidence: |
| GO:0031410 cytoplasmic vesicle | IDA PMID:22792322 The E3-ubiquitin ligase TRIM50 interacts with HDAC6 and p62,... | KEEP AS NON CORE | Summary: Retain the experimental vesicle-associated pool. Reason: The source-specific annotation is compatible with independently supported CAV1 cytoplasmic vesicles. The exact individual localization image in the TRIM50 study is not independently inspected. |
| GO:0031623 receptor internalization | IDA PMID:25893292 Syntenin regulates TGF-Ξ²1-induced Smad activation and the ep... | KEEP AS NON CORE | Summary: CAV1 contributes to receptor internalization in defined signaling contexts. Reason: The respective studies describe CAV1-associated receptor uptake in TGF-beta or Wnt signaling. Retain the contextual process without assigning receptor catalytic activity or claiming all internalization requires caveolae. |
| GO:0031623 receptor internalization | IMP PMID:16890161 Caveolin is necessary for Wnt-3a-dependent internalization o... | KEEP AS NON CORE | Summary: CAV1 contributes to receptor internalization in defined signaling contexts. Reason: The respective studies describe CAV1-associated receptor uptake in TGF-beta or Wnt signaling. Retain the contextual process without assigning receptor catalytic activity or claiming all internalization requires caveolae. |
| GO:0031901 early endosome membrane | TAS Reactome:R-HSA-5368596 | KEEP AS NON CORE | Summary: Early endosomal residence is compatible with LRP6 trafficking. Reason: The curated WNT3A-LRP6 internalization event supports a receptor-trafficking compartment. This is a transient membrane pool, not the only site of CAV1 function. Supporting Evidence: Reactome:R-HSA-5368596 |
| GO:0032507 maintenance of protein location in cell | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: CAV1 can retain proteins at particular membrane locations. Reason: The rat ortholog transfer agrees with human TRPC1 surface-retention experiments. Those experiments support the general role without reproducing the original rat donor assay or implying universal retention of all partners. Supporting Evidence: |
| GO:0032570 response to progesterone | IDA PMID:12388746 Caveolin-1-deficient mice show accelerated mammary gland dev... | KEEP AS NON CORE | Summary: Retain the hormone-responsive CAV1 context with experimental curator deference. Reason: Selected external Results explicitly test hTERT-HME1 human mammary epithelial cells: progesterone alone mildly lowers CAV1 protein, whereas estrogen plus progesterone increases it. This is a stimulus response, not progesterone-receptor activity or a uniform positive direction. The canonical cache remains abstract-only. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:21822278 Endolysosomal sorting of ubiquitylated caveolin-1 is regulat... | KEEP AS NON CORE | Summary: CAV1 occurs in a VCP-UBXD1-associated complex. Reason: The protein is a ubiquitin-dependent trafficking substrate within this assembly. Complex association does not make CAV1 a VCP ATPase or the cargo-processing catalyst. Supporting Evidence: |
| GO:0032991 protein-containing complex | IDA PMID:24013648 Molecular composition and ultrastructure of the caveolar coa... | ACCEPT | Summary: CAV1 is part of a biochemically isolated coat complex. Reason: Human HeLa cross-linking, immunoisolation and mass spectrometry establish a caveolin-cavin coat assembly. CAV1/CAV2 and cavin contributions are distinguished; the measured sedimentation and estimated ratios are preparation-dependent. Supporting Evidence: PMID:24013648 caveolins and cavins can be purified as a single species of protein complex |
| GO:0032991 protein-containing complex | IEA GO_REF:0000107 | ACCEPT | Summary: The broad protein-complex location has direct human support. Reason: The mouse-derived annotation agrees with human caveolin-cavin coat isolation. A broad complex assertion does not identify every interaction partner as a constitutive coat component. Supporting Evidence: |
| GO:0033484 intracellular nitric oxide homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: NO homeostasis is a consequence of CAV1-dependent NOS regulation. Reason: CAV1-derived peptides and full-length cellular experiments support inhibition of NOS, with calmodulin-dependent release. This supports regulation of NO abundance without assigning NO-synthesis catalysis to CAV1. |
| GO:0036487 nitric-oxide synthase inhibitor activity | EXP PMID:9325253 Dissecting the interaction between nitric oxide synthase (NO... | ACCEPT | Summary: CAV1 directly inhibits nitric-oxide synthase in defined assays. Reason: The externally read primary Methods/Results combine binding controls, inhibitory scaffolding-domain peptide assays and full-length cellular eNOS coexpression. Bovine eNOS, rat nNOS and human iNOS experiments are distinct; peptide inhibition does not establish equivalent native regulation of every isoform. Supporting Evidence: PMID:9325253 suppress NO release in co-transfection experiments |
| GO:0036487 nitric-oxide synthase inhibitor activity | EXP PMID:9712842 Interaction between caveolin-1 and the reductase domain of e... | ACCEPT | Summary: NOS inhibition includes an effect on reductase-dependent electron transfer. Reason: The primary indexed Results compare NO formation, NADPH oxidation, cytochrome-c and ferricyanide reduction and a control peptide. They support inhibitory regulation beyond simple competition at an oxygenase-domain motif; a native atomic complex and exact construct species were not resolved. Supporting Evidence: PMID:9712842 Cav-1P equivalently inhibited NO synthesis and NADPH oxidation |
| GO:0036487 nitric-oxide synthase inhibitor activity | IEA GO_REF:0000107 | ACCEPT | Summary: The conserved NOS-inhibitory assignment has direct mechanistic support. Reason: Independent CAV1 biochemical and cellular experiments support this inhibitory function. The mouse transfer is retained without claiming the donor assay or ancestral mechanism was reproduced. |
| GO:0038016 insulin receptor internalization | IEA GO_REF:0000107 | UNDECIDED | Summary: The particular insulin-receptor internalization transfer is unresolved. Reason: The exact mouse receptor-trafficking experiment was not accessed. General caveolar trafficking or the effect of CAV1 loss on metabolism does not independently establish this specific receptor endpoint. |
| GO:0038166 angiotensin-activated signaling pathway | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific angiotensin-signaling transfer requires source-level resolution. Reason: The mouse cardiac context may involve CAV1-dependent signaling complexes, but the actual angiotensin perturbation and causal step were not inspected. No direct receptor or ligand activity is inferred. |
| GO:0038166 angiotensin-activated signaling pathway | ISS GO_REF:0000024 | UNDECIDED | Summary: The specific angiotensin-signaling transfer requires source-level resolution. Reason: The mouse cardiac context may involve CAV1-dependent signaling complexes, but the actual angiotensin perturbation and causal step were not inspected. No direct receptor or ligand activity is inferred. |
| GO:0042383 sarcolemma | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the inherited muscle-cell membrane context with a node-audit limit. Reason: CAV1 is observed in human myometrial caveolar membrane complexes. The sarcolemma assertion is therefore not rejected merely because several PAINT donors are caveolin paralogs. The precise ancestral placement and transfer across muscle subtypes remain uninspected. Supporting Evidence: |
| GO:0042632 cholesterol homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Cholesterol homeostasis is a supported membrane-trafficking role. Reason: CAV1-associated raft trafficking and ABCG1-dependent efflux support cholesterol handling. This broad process does not assign CAV1 cholesterol biosynthesis or ATP-driven transport chemistry. |
| GO:0042632 cholesterol homeostasis | TAS PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | KEEP AS NON CORE | Summary: Cholesterol homeostasis is a supported membrane-trafficking role. Reason: CAV1-associated raft trafficking and ABCG1-dependent efflux support cholesterol handling. This broad process does not assign CAV1 cholesterol biosynthesis or ATP-driven transport chemistry. |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 self-association supports oligomeric coat assembly. Reason: Oligomerization and disruption by the tested C156S construct support the self-association assertion. The binding term is retained as less informative than the structural assembly role; it does not establish a universal oligomer stoichiometry. |
| GO:0042802 identical protein binding | IPI PMID:25006397 Nitrosation-dependent caveolin 1 phosphorylation, ubiquitina... | KEEP AS NON CORE | Summary: CAV1 self-association supports oligomeric coat assembly. Reason: Oligomerization and disruption by the tested C156S construct support the self-association assertion. The binding term is retained as less informative than the structural assembly role; it does not establish a universal oligomer stoichiometry. |
| GO:0043123 positive regulation of canonical NF-kappaB signal transduction | IMP PMID:23319823 Downregulation of miR-138 sustains NF-ΞΊB activation and prom... | KEEP AS NON CORE | Summary: Canonical NF-kappaB regulation is a contextual signaling outcome. Reason: The experimental source supports positive regulation in its tested setting. CAV1 organizes signaling partners rather than supplying NF-kappaB DNA binding or kinase catalysis. Supporting Evidence: |
| GO:0043409 negative regulation of MAPK cascade | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the mouse-derived negative MAPK-regulatory context. Reason: The cached primary abstract and selected external Results report hyperactivation of ERK1/2 in pregnant Cav1-null mouse mammary glands. This independently supports the negative-regulatory mouse context; it does not establish direct inhibition of every MAPK or a universal effect in human tissues. Supporting Evidence: |
| GO:0043627 response to estrogen | IDA PMID:12388746 Caveolin-1-deficient mice show accelerated mammary gland dev... | KEEP AS NON CORE | Summary: Retain the hormone-responsive CAV1 context with experimental curator deference. Reason: Selected external Results explicitly test hTERT-HME1 human mammary epithelial cells. Estrogen alone does not change CAV1 protein in the reported assay, whereas combined estrogen and progesterone increases it. Retain the experimentally curated response in that combined-hormone context, without asserting estrogen binding or an estrogen-alone induction. The canonical cache remains abstract-only. Supporting Evidence: |
| GO:0044325 transmembrane transporter binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Transporter association has direct CAV1 evidence. Reason: Human hERG binding and TRPC1 association support this PAINT function. The target descendant is valid support; the ancestral node was not independently examined. Binding does not assign conductance to CAV1. |
| GO:0044325 transmembrane transporter binding | IPI PMID:18923542 The regulation of the cardiac potassium channel (HERG) by ca... | KEEP AS NON CORE | Summary: The hERG interaction supports transporter binding. Reason: The complete abstract describes yeast two-hybrid screening of a human-heart library, coimmunoprecipitation and functional HEK293 assays. No native cardiac complex stoichiometry or purified interface is inferred. Supporting Evidence: |
| GO:0044860 protein localization to plasma membrane raft | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: CAV1 helps organize selected proteins in membrane domains. Reason: The canine ortholog transfer is consistent with direct CAV1-dependent recruitment and retention of human signaling proteins. It is retained as a general localization role without asserting universal partitioning into detergent-resistant rafts. |
| GO:0044877 protein-containing complex binding | IPI PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: Retain association with an ERAD protein assembly. Reason: The available source describes CAV1 association with p97-containing complexes and enhanced partner recruitment. The broad complex-binding annotation does not make CAV1 an ATPase, ubiquitin ligase or obligatory structural subunit of all ERAD complexes. Supporting Evidence: |
| GO:0045019 negative regulation of nitric oxide biosynthetic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: CAV1 can reduce NO production through NOS inhibition. Reason: Direct inhibitory NOS experiments support this downstream process. The direction can change when CAV1 is displaced or modified; it is not universal suppression in every cell state. |
| GO:0045121 membrane raft | IDA PMID:11294831 BENE, a novel raft-associated protein of the MAL proteolipid... | ACCEPT | Summary: Retain CAV1 in cholesterol-rich membrane domains. Reason: The human BENE study describes CAV1-associated raft trafficking and redistribution after cholesterol oxidation. Detergent fractionation and colocalization do not imply that every raft is a morphologic caveola. Supporting Evidence: PMID:11294831 migrated to the plasmalemma accompanying caveolin-1 |
| GO:0045121 membrane raft | IDA PMID:14559243 Association of the calpain/calpastatin network with subcellu... | ACCEPT | Summary: The experimentally curated raft location is retained. Reason: The source assignment agrees with independent human CAV1 raft/caveolar evidence. The exact original fractionation controls are not re-inspected; no direct chemical-affinity claim is derived from localization. |
| GO:0045121 membrane raft | IDA PMID:17010968 The shedding activity of ADAM17 is sequestered in lipid raft... | ACCEPT | Summary: Retain the membrane-raft CAV1 pool in this experimental context. Reason: The annotated localization is consistent with independent human CAV1 raft trafficking. The source-specific preparation does not establish a universal membrane-domain composition. |
| GO:0045121 membrane raft | IDA PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | ACCEPT | Summary: CAV1 occurs in raft-associated apoptotic signaling assemblies. Reason: The hyperoxia study examines CAV1-associated Fas/BID signaling and raft recruitment. This location is retained while keeping cell-death effects context dependent. Supporting Evidence: |
| GO:0045121 membrane raft | IDA PMID:23262137 The myosin motor Myo1c is required for VEGFR2 delivery to th... | ACCEPT | Summary: Retain the plasma-membrane raft pool. Reason: The source supports membrane-domain localization, consistent with independent caveolar coat evidence. Raft association does not make every resident partner a caveolar structural component. |
| GO:0045121 membrane raft | IDA PMID:24576892 Caveolin-1 interacts with ATP binding cassette transporter G... | ACCEPT | Summary: CAV1 occupies the membrane domains involved in ABCG1-linked efflux. Reason: The transporter study reports CAV1 association with ABCG1 and raft-related cholesterol handling. Transport catalysis remains assigned to ABCG1. Supporting Evidence: |
| GO:0045121 membrane raft | IDA PMID:25204797 Flotillin-1 facilitates toll-like receptor 3 signaling in hu... | ACCEPT | Summary: Retain the curated raft localization with bounded access. Reason: The exact original target-specific fractionation panel is uninspected, but independent human CAV1 raft localization supports the location. No source misattribution is inferred from the limited cache. |
| GO:0045121 membrane raft | IDA PMID:25893292 Syntenin regulates TGF-Ξ²1-induced Smad activation and the ep... | ACCEPT | Summary: CAV1-containing membrane domains participate in receptor trafficking. Reason: The source describes caveolar versus other TGF-beta receptor trafficking routes. This supports the membrane-domain pool without asserting a single route for every receptor molecule. Supporting Evidence: PMID:25893292 internalization of TΞ²RI and caveolin-1 from lipid rafts |
| GO:0045121 membrane raft | IEA GO_REF:0000120 | ACCEPT | Summary: The conserved raft-associated membrane pool is well supported. Reason: The combined electronic location mapping names the mouse ortholog P49817 and the membrane-raft location entry. It agrees with direct human CAV1 membrane-domain evidence. The exact donor assay and individual combined-rule logic were not re-inspected; this row does not name the bovine donor of the separate ISS assertion. |
| GO:0045121 membrane raft | ISS GO_REF:0000024 | ACCEPT | Summary: The conserved raft-associated membrane pool is well supported. Reason: The electronic location mapping and bovine ortholog transfer agree with direct human CAV1 membrane-domain evidence. The exact donor assay and individual combined-rule logic were not re-inspected. |
| GO:0045907 positive regulation of vasoconstriction | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Vasoconstriction regulation is a plausible physiological consequence of NOS restraint. Reason: CAV1-dependent NOS inhibition supports regulation of vascular tone. Retain the curated mouse transfer as a contextual outcome without asserting that CAV1 itself contracts smooth muscle or that the original vessel assay was re-read. |
| GO:0046209 nitric oxide metabolic process | TAS Reactome:R-HSA-203615 | KEEP AS NON CORE | Summary: CAV1 regulates NO metabolism through an enzyme interaction. Reason: The curated nitric-oxide pathway includes inhibition and release of eNOS. CAV1 contributes regulatory work but does not catalyze conversion of arginine to NO. |
| GO:0046426 negative regulation of receptor signaling pathway via JAK-STAT | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the prolactin/JAK-STAT inhibitory context. Reason: The cached primary abstract and selected external Results describe CAV1-dependent attenuation of prolactin/JAK2/STAT5 signaling, with mouse HC11 reporter assays and hyperphosphorylation in Cav1-null mammary glands. Retain the mouse-derived pathway regulation without claiming that CAV1 is a kinase or that these are native human signaling experiments. Supporting Evidence: |
| GO:0046982 protein heterodimerization activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain caveolin hetero-association without a fixed dimer model. Reason: CAV1 and CAV2 occur in the isolated human coat complex, consistent with the curated heterodimerization transfer. The preparation does not establish that the only relevant assembly is a discrete heterodimer. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the inherited perinuclear trafficking pool. Reason: The MLC1 study uses human and rat astrocytes, but its abstract foregrounds MLC1 localization rather than exposing every CAV1 image. The broad perinuclear CAV1 pool is retained with explicit experimental/phylogenetic curator deference and consistency with intracellular CAV1 trafficking; the exact original compartment-marker panel and donor assay are uninspected. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:19931615 MLC1 trafficking and membrane expression in astrocytes: role... | KEEP AS NON CORE | Summary: Perinuclear CAV1 is a trafficking-associated pool. Reason: The MLC1 study uses human and rat astrocytes, but its abstract foregrounds MLC1 localization rather than exposing every CAV1 image. The broad perinuclear CAV1 pool is retained with explicit experimental/phylogenetic curator deference and consistency with intracellular CAV1 trafficking; the exact original compartment-marker panel and donor assay are uninspected. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Perinuclear CAV1 is a trafficking-associated pool. Reason: The MLC1 study uses human and rat astrocytes, but its abstract foregrounds MLC1 localization rather than exposing every CAV1 image. The broad perinuclear CAV1 pool is retained with explicit experimental/phylogenetic curator deference and consistency with intracellular CAV1 trafficking; the exact original compartment-marker panel and donor assay are uninspected. Supporting Evidence: |
| GO:0048471 perinuclear region of cytoplasm | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Perinuclear CAV1 is a trafficking-associated pool. Reason: The MLC1 study uses human and rat astrocytes, but its abstract foregrounds MLC1 localization rather than exposing every CAV1 image. The broad perinuclear CAV1 pool is retained with explicit experimental/phylogenetic curator deference and consistency with intracellular CAV1 trafficking; the exact original compartment-marker panel and donor assay are uninspected. Supporting Evidence: |
| GO:0048550 negative regulation of pinocytosis | IMP PMID:23583380 Prominin-2 expression increases protrusions, decreases caveo... | KEEP AS NON CORE | Summary: CAV1 restrains pinocytosis in the tested prominin-2 context. Reason: The abstract reports that CAV1 downregulation restores macropinocytic activity in prominin-2-expressing cells. This supports the specific inhibitory context rather than universal inhibition of endocytosis. Supporting Evidence: |
| GO:0050998 nitric-oxide synthase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: NOS binding is supported but less informative than inhibitory regulation. Reason: The source describes eNOS-CAV1 association; independent biochemical work supports physical and functional interaction. Keep the binding assertion without multiplying it into a redundant core function. |
| GO:0050998 nitric-oxide synthase binding | IPI PMID:12852865 Caveolae and caveolin-1 in human term villous trophoblast. | KEEP AS NON CORE | Summary: NOS binding is supported but less informative than inhibitory regulation. Reason: The source describes eNOS-CAV1 association; independent biochemical work supports physical and functional interaction. Keep the binding assertion without multiplying it into a redundant core function. |
| GO:0051117 ATPase binding | IPI PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: p97 association supports ATPase binding. Reason: The available Discussion explicitly reports CAV1 interaction with p97 and coordinated recruitment within COX2 ERAD. This does not transfer p97 ATPase activity to CAV1. Original Results and Methods are absent from this cached HTML extraction. Supporting Evidence: |
| GO:0051117 ATPase binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the conserved ATPase-interaction context. Reason: Independent human CAV1-p97 association supports the broad binding function while the precise bovine donor assay remains uninspected. ATP hydrolysis is performed by the partner ATPase. Supporting Evidence: |
| GO:0051480 regulation of cytosolic calcium ion concentration | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: CAV1 regulates cytosolic calcium through channel organization. Reason: The human TRPC1 experiments support the PAINT process. A target descendant is legitimate support; the actual ancestral placement was not read. This does not make CAV1 a calcium pore. |
| GO:0051480 regulation of cytosolic calcium ion concentration | IDA PMID:19052258 Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to... | KEEP AS NON CORE | Summary: CAV1 modulates calcium entry through the TRPC1 complex. Reason: Knockout/rescue and channel-association experiments establish context-dependent changes in calcium entry. A CSD deletion can increase entry while reducing association, so the process is summarized as regulation rather than a universal activation rule. Supporting Evidence: |
| GO:0051592 response to calcium ion | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain calcium-responsive complex organization in the studied setting. Reason: The annotated response is consistent with store depletion and calcium-entry-linked reorganization of CAV1-associated channels. It does not establish CAV1 as a calcium sensor or prove direct calcium binding. |
| GO:0051592 response to calcium ion | ISS PMID:19052258 Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to... | KEEP AS NON CORE | Summary: Retain calcium-responsive complex organization in the studied setting. Reason: The annotated response is consistent with store depletion and calcium-entry-linked reorganization of CAV1-associated channels. It does not establish CAV1 as a calcium sensor or prove direct calcium binding. |
| GO:0051899 membrane depolarization | ISS GO_REF:0000024 | UNDECIDED | Summary: The exact membrane-depolarization transfer is unresolved. Reason: The mouse donor membrane and channel context were not inspected. Regulation of hERG or TRPC1 cannot by itself establish depolarization in the particular annotated cell type. |
| GO:0055074 calcium ion homeostasis | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: CAV1 supports calcium homeostasis through channel-complex organization. Reason: Independent human TRPC1 surface-retention and calcium-entry evidence supports this broad mouse-derived process. The detailed donor experiment was not re-read, and CAV1 is not itself the conducting channel. |
| GO:0060056 mammary gland involution | ISS GO_REF:0000024 | UNDECIDED | Summary: The specific mammary-involution role requires donor-level evidence. Reason: Selected external Results report sustained STAT5 phosphorylation after weaning but no observed extension of lactation by the stated morphological criteria; the authors leave direct involution involvement versus compensation unresolved. The source-specific donor assignment therefore remains uncertain, not disproved by a broad expression or apoptosis argument. Supporting Evidence: |
| GO:0060070 canonical Wnt signaling pathway | IDA PMID:16890161 Caveolin is necessary for Wnt-3a-dependent internalization o... | KEEP AS NON CORE | Summary: CAV1 participates in the tested canonical Wnt signaling route. Reason: LRP6 association and CAV1-dependent internalization support the contextual process. This is membrane organization and receptor trafficking rather than a Wnt ligand or transcription-factor activity. Supporting Evidence: |
| GO:0060090 molecular adaptor activity | IBA GO_REF:0000033 | MODIFY | Summary: Refine the broad adaptor term to protein-macromolecule adaptor activity. Reason: Human CAV1 organizes interactions among proteins in membrane-associated assemblies. This is a supported specialization of the inherited adaptor function; it does not claim that the original PAINT node was inspected or found defective. Proposed replacements: protein-macromolecule adaptor activity |
| GO:0060090 molecular adaptor activity | IEA GO_REF:0000107 | MODIFY | Summary: Protein-macromolecule adaptor activity describes the supported scaffold function. Reason: CAV1 promotes coordinated localization and association of channel-complex components. It is not the pore or the activating STIM1 sensor; the more specific adaptor term preserves the essence of the source assertion. Proposed replacements: protein-macromolecule adaptor activity |
| GO:0060090 molecular adaptor activity | TAS PMID:19052258 Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to... | MODIFY | Summary: Protein-macromolecule adaptor activity describes the supported scaffold function. Reason: CAV1 promotes coordinated localization and association of channel-complex components. It is not the pore or the activating STIM1 sensor; the more specific adaptor term preserves the essence of the source assertion. Proposed replacements: protein-macromolecule adaptor activity |
| GO:0060546 negative regulation of necroptotic process | IEA GO_REF:0000107 | UNDECIDED | Summary: The transferred necroptosis-specific effect is unresolved. Reason: The mouse donor death-pathway controls were not accessed. Apoptosis or anoikis assays elsewhere in this review cannot substitute for a necroptosis-specific mechanism. |
| GO:0070320 inward rectifier potassium channel inhibitor activity | IDA PMID:18923542 The regulation of the cardiac potassium channel (HERG) by ca... | KEEP AS NON CORE | Summary: Retain the experimentally supported hERG inhibitory activity. Reason: The complete abstract reports physical CAV1-hERG association and reciprocal effects of CAV1 knockdown and overexpression on current amplitude and deactivation in HEK293/HERG cells. The inward-rectifier wording is retained with experimental curator deference, without confusing CAV1 with the pore or claiming native cardiomyocyte measurements. Supporting Evidence: |
| GO:0070836 caveola assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Caveolar assembly is a defining conserved CAV1 role. Reason: Human coat biochemistry and structural localization independently support the PAINT process. Paralogs and target descendant evidence in WITH/FROM do not establish a propagation failure; the ancestral placement itself was not inspected. Supporting Evidence: |
| GO:0070836 caveola assembly | IEA GO_REF:0000002 | ACCEPT | Summary: The InterPro mapping agrees with CAV1 coat assembly. Reason: The caveolin family assignment is supported by direct human CAV1 coat organization. This electronic inference is not accepted solely because a domain name resembles the process. Supporting Evidence: |
| GO:0070836 caveola assembly | IGI PMID:25006397 Nitrosation-dependent caveolin 1 phosphorylation, ubiquitina... | ACCEPT | Summary: Human CAV1 constructs support caveolar assembly in the tested rescue context. Reason: The study combines human CAV1-GFP construct experiments with mouse CAV1-null endothelial rescue. The C156S substitution affects oligomerization and localization as well as partner association; those effects are not separated into a pure binding defect. Supporting Evidence: PMID:25006397 WT-Cav-1 cDNA was sufficient to induce formation of caveolae |
| GO:0070836 caveola assembly | IMP PMID:12633858 Involvement of caveolin-2 in caveolar biogenesis in MDCK cel... | ACCEPT | Summary: Retain the experimentally established CAV1 contribution to caveola assembly. Reason: The source tests CAV1-dependent caveolar organization. Independent human coat isolation supports actual structural participation rather than necessity alone. The exact original figure panels were not all accessible. Supporting Evidence: PMID:12633858 caveolin-1 and -2 are found together on basolateral caveolae |
| GO:0070836 caveola assembly | ISS GO_REF:0000024 | ACCEPT | Summary: The ortholog-derived caveolar assembly function is directly supported in human cells. Reason: Canine and mouse donor assertions are preserved. Human CAV1 physically participates in coat organization, so the process does not rest only on mutant necessity or a partner phenotype. Supporting Evidence: |
| GO:0070836 caveola assembly | ISS GO_REF:0000024 | ACCEPT | Summary: The ortholog-derived caveolar assembly function is directly supported in human cells. Reason: Canine and mouse donor assertions are preserved. Human CAV1 physically participates in coat organization, so the process does not rest only on mutant necessity or a partner phenotype. Supporting Evidence: |
| GO:0071218 cellular response to misfolded protein | IMP PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: Retain the ERAD-related misfolded-protein response context. Reason: The source describes CAV1-associated handling of COX2 through ERAD machinery. It supports a contextual protein-quality-control role, without making CAV1 a general folding chaperone or protease. The cached HTML lacks original Methods/Results. Supporting Evidence: |
| GO:0071375 cellular response to peptide hormone stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Peptide-hormone signaling can reorganize CAV1-associated complexes. Reason: The broad transfer is consistent with receptor-linked phosphorylation, trafficking and membrane signaling. Retain the contextual response with curator deference, without assigning hormone-binding receptor activity to CAV1. |
| GO:0071375 cellular response to peptide hormone stimulus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Peptide-hormone signaling can reorganize CAV1-associated complexes. Reason: The broad transfer is consistent with receptor-linked phosphorylation, trafficking and membrane signaling. Retain the contextual response with curator deference, without assigning hormone-binding receptor activity to CAV1. |
| GO:0071455 cellular response to hyperoxia | IMP PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | KEEP AS NON CORE | Summary: CAV1 participates in the tested hyperoxic stress response. Reason: The source examines CAV1-dependent Fas/BID signaling under hyperoxia. This is a stress-specific outcome and is not generalized to hypoxia or every apoptotic stimulus. Supporting Evidence: |
| GO:0072584 caveolin-mediated endocytosis | IDA PMID:19931615 MLC1 trafficking and membrane expression in astrocytes: role... | KEEP AS NON CORE | Summary: MLC1-associated caveolar trafficking is retained as a context-dependent, non-core process. Reason: Newly accessed original Results and Fig. 8 caption show a target perturbation: human U251 cells expressing His-MLC1 received CAV1-GFP or GFP control. After ten days, excess CAV1 reduced the cytosolic MLC1 fraction and MLC1/CAV1-positive intracellular vesicles; pharmacological raft-trafficking manipulations provided complementary evidence. Association and vesicular localization were separately demonstrated, including in rat astrocytes. Retain the curated IDA with explicit deference to this combined target/cargo evidence as a non-core context. The overexpression phenotype is inhibitory and does not directly measure vesicle pinching or establish that every CAV1 pool promotes uptake. Original image pixels and supplements remain uninspected. The short cached anchor describes the cargo; the newly inspected target controls are documented separately in the notes. Supporting Evidence: PMID:19931615 undergoes caveolae/raft-mediated endocytosis |
| GO:0086091 regulation of heart rate by cardiac conduction | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific cardiac-conduction rate transfer is unresolved. Reason: The mouse donor physiological recordings and cell type were not accessed. Heterologous hERG current effects do not independently demonstrate regulation of heart rate by cardiac conduction. |
| GO:0086091 regulation of heart rate by cardiac conduction | ISS GO_REF:0000024 | UNDECIDED | Summary: The specific cardiac-conduction rate transfer is unresolved. Reason: The mouse donor physiological recordings and cell type were not accessed. Heterologous hERG current effects do not independently demonstrate regulation of heart rate by cardiac conduction. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | IEA GO_REF:0000107 | UNDECIDED | Summary: The negative Wnt-transfer context needs its original donor evidence. Reason: The human LRP6 study supports a positive receptor-internalization signaling route. CAV1 may exert different effects in other settings, but the exact mouse negative pathway experiment was not inspected; the opposite direction is not rejected solely from that difference. |
| GO:0090090 negative regulation of canonical Wnt signaling pathway | ISS GO_REF:0000024 | UNDECIDED | Summary: The negative Wnt-transfer context needs its original donor evidence. Reason: The human LRP6 study supports a positive receptor-internalization signaling route. CAV1 may exert different effects in other settings, but the exact mouse negative pathway experiment was not inspected; the opposite direction is not rejected solely from that difference. |
| GO:0097190 apoptotic signaling pathway | IMP PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | KEEP AS NON CORE | Summary: Retain the stress-dependent apoptotic signaling role. Reason: The cited source supports CAV1-associated Fas/BID signaling in hyperoxia. This is distinct from the protective MCL1/anoikis context and is not a universal proapoptotic function. Supporting Evidence: |
| GO:0098903 regulation of membrane repolarization during action potential | IMP PMID:18923542 The regulation of the cardiac potassium channel (HERG) by ca... | KEEP AS NON CORE | Summary: hERG regulation supports a repolarization-related consequence. Reason: The human hERG/HEK293 study links CAV1 association to altered current and deactivation, providing a mechanism relevant to repolarizing current. Retain the existing broad experimental process with curator deference as a non-core consequence. Native cardiac action-potential or contraction recordings were not recovered, so this decision does not resolve the separately annotated contraction-coupled cardiac endpoint. Supporting Evidence: |
| GO:0098909 regulation of cardiac muscle cell action potential involved in regulation of contraction | IMP PMID:18923542 The regulation of the cardiac potassium channel (HERG) by ca... | UNDECIDED | Summary: The contraction-coupled cardiac action-potential scope remains unresolved. Reason: The complete abstract documents human hERG/HEK293 electrophysiology but not native cardiac contraction or action-potential coupling. Full-text native-tissue experiments were not recovered; the specific IMP assertion is preserved as uncertain rather than removed from an abstract omission. Supporting Evidence: |
| GO:0098911 regulation of ventricular cardiac muscle cell action potential | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific ventricular-cell action-potential transfer is unresolved. Reason: The original mouse electrophysiology and distinction between direct CAV1 effects and altered tissue organization were not accessed. Human heterologous hERG experiments do not independently establish the ventricular-cell endpoint. |
| GO:0098911 regulation of ventricular cardiac muscle cell action potential | ISS GO_REF:0000024 | UNDECIDED | Summary: The specific ventricular-cell action-potential transfer is unresolved. Reason: The original mouse electrophysiology and distinction between direct CAV1 effects and altered tissue organization were not accessed. Human heterologous hERG experiments do not independently establish the ventricular-cell endpoint. |
| GO:0120162 positive regulation of cold-induced thermogenesis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain cold thermogenesis as a mouse-derived physiological context. Reason: The source describes impaired cold adaptation and brown-adipose physiology in CAV1-deficient mice. This is a non-core outcome of lipid and membrane organization; CAV1 is not assigned uncoupling-protein transport or heat-generating enzyme activity. Supporting Evidence: |
| GO:0120162 positive regulation of cold-induced thermogenesis | ISS PMID:15734843 Caveolin-1 expression is essential for proper nonshivering t... | KEEP AS NON CORE | Summary: Retain cold thermogenesis as a mouse-derived physiological context. Reason: The source describes impaired cold adaptation and brown-adipose physiology in CAV1-deficient mice. This is a non-core outcome of lipid and membrane organization; CAV1 is not assigned uncoupling-protein transport or heat-generating enzyme activity. Supporting Evidence: |
| GO:0140311 protein sequestering activity | ISS PMID:19265160 The heme oxygenase-1/carbon monoxide pathway suppresses TLR4... | KEEP AS NON CORE | Summary: Retain the curated protein-sequestering context with bounded access. Reason: The murine source abstract reports motif-dependent CAV1-TLR4 binding and inhibition of inflammatory signaling. Production GO-CAM 645d887900001414 explicitly models this as CAV1 protein sequestering with TLR4 as input, using the same mouse-to-human evidence. Retain this context with curator deference; exact partner-exclusion controls are not visible in the abstract, and no generic sequestration of all CAV1 partners is inferred. Supporting Evidence: |
| GO:1900027 regulation of ruffle assembly | IDA PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | KEEP AS NON CORE | Summary: CAV1 regulates ruffling through a small-GTPase signaling context. Reason: The source relates CAV1-RAC1 association to membrane ruffling and bacterial uptake. CAV1 does not thereby become an actin polymerase or a Rho-family GTPase. Supporting Evidence: |
| GO:1901380 negative regulation of potassium ion transmembrane transport | IMP PMID:18923542 The regulation of the cardiac potassium channel (HERG) by ca... | KEEP AS NON CORE | Summary: CAV1 can reduce hERG-mediated potassium flux. Reason: Knockdown and overexpression have reciprocal effects on hERG currents in HEK293 cells. This supports a regulatory effect; potassium conduction is performed by hERG and the native myocardial mechanism is not independently established by the abstract. Supporting Evidence: |
| GO:1901844 regulation of cell communication by electrical coupling involved in cardiac conduction | IEA GO_REF:0000107 | UNDECIDED | Summary: The specific electrical-coupling transfer needs its donor experiments. Reason: Mouse CAV1-dependent cardiac signaling may affect junctional organization, but the actual coupling measurements and causal cell-type context were not accessed. A hERG current change is not itself evidence of gap-junction coupling. |
| GO:1901844 regulation of cell communication by electrical coupling involved in cardiac conduction | ISS GO_REF:0000024 | UNDECIDED | Summary: The specific electrical-coupling transfer needs its donor experiments. Reason: Mouse CAV1-dependent cardiac signaling may affect junctional organization, but the actual coupling measurements and causal cell-type context were not accessed. A hERG current change is not itself evidence of gap-junction coupling. |
| GO:1903361 protein localization to basolateral plasma membrane | ISS GO_REF:0000024 | UNDECIDED | Summary: The basolateral targeting assertion needs its polarized-cell donor assay. Reason: The specified canine donor is retained. General CAV1 membrane localization and trafficking do not alone resolve polarized basolateral sorting or its cargo specificity. |
| GO:1903598 positive regulation of gap junction assembly | IEA GO_REF:0000107 | UNDECIDED | Summary: The positive gap-junction assembly transfer is not independently resolved. Reason: The mouse donor experiment separating junction assembly from protein expression, turnover or electrical coupling was not accessed. The source assertion is preserved without assigning CAV1 connexin pore activity. |
| GO:1903598 positive regulation of gap junction assembly | ISS GO_REF:0000024 | UNDECIDED | Summary: The positive gap-junction assembly transfer is not independently resolved. Reason: The mouse donor experiment separating junction assembly from protein expression, turnover or electrical coupling was not accessed. The source assertion is preserved without assigning CAV1 connexin pore activity. |
| GO:1904294 positive regulation of ERAD pathway | IMP PMID:24089527 Caveolin-1 interacts with Derlin-1 and promotes ubiquitinati... | KEEP AS NON CORE | Summary: CAV1 can promote assembly of COX2-associated ERAD machinery. Reason: The available primary Discussion describes CAV1-dependent association of COX2, Derlin-1, p97 and Ufd1 during ubiquitination and degradation. This is organizing work, not proteolytic or ubiquitin-ligase catalysis by CAV1; the cache omits original Results/Methods. Supporting Evidence: |
| GO:2000535 regulation of entry of bacterium into host cell | IDA PMID:24625804 Caveolin-1 mediates Salmonella invasion via the regulation o... | KEEP AS NON CORE | Summary: CAV1 regulates bacterial entry in the tested membrane-signaling model. Reason: The source links CAV1-RAC1 organization and ruffling to bacterial uptake. The direction and organism context are source specific; other CAV1 pathways can prevent rather than promote entry. Supporting Evidence: |
| GO:2000811 negative regulation of anoikis | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: CAV1 can suppress detachment-induced apoptosis through MCL1 stabilization. Reason: Human H460/G361 perturbations, viability/apoptotic morphology and MCL1 ubiquitination assays support this context. Steric shielding is proposed, not structurally demonstrated. These cancer-cell results do not establish universal antiapoptotic action. Supporting Evidence: |
| GO:2000811 negative regulation of anoikis | IMP PMID:22277751 Caveolin-1 regulates Mcl-1 stability and anoikis in lung car... | KEEP AS NON CORE | Summary: CAV1 can suppress detachment-induced apoptosis through MCL1 stabilization. Reason: Human H460/G361 perturbations, viability/apoptotic morphology and MCL1 ubiquitination assays support this context. Steric shielding is proposed, not structurally demonstrated. These cancer-cell results do not establish universal antiapoptotic action. Supporting Evidence: |
| GO:2001238 positive regulation of extrinsic apoptotic signaling pathway | IMP PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | KEEP AS NON CORE | Summary: Retain the source-specific proapoptotic Fas/BID signaling contributions. Reason: The hyperoxia study relates CAV1 to extrinsic Fas signaling and BID-associated intrinsic signaling. The assertions are retained as coupled stress-context outcomes, without treating CAV1 as a caspase or mitochondrial pore-forming effector. Supporting Evidence: |
| GO:2001244 positive regulation of intrinsic apoptotic signaling pathway | IMP PMID:21382479 Caveolin-1 mediates Fas-BID signaling in hyperoxia-induced a... | KEEP AS NON CORE | Summary: Retain the source-specific proapoptotic Fas/BID signaling contributions. Reason: The hyperoxia study relates CAV1 to extrinsic Fas signaling and BID-associated intrinsic signaling. The assertions are retained as coupled stress-context outcomes, without treating CAV1 as a caspase or mitochondrial pore-forming effector. Supporting Evidence: |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Should integral CAV1 coat scaffolding be represented explicitly by GO:0140378 in source annotation, separately from the existing adaptor assertions? The structural core is supported by target assembly evidence, but exact same-role CAVIN1/CLTC/BIN1 annotation comparators were not fully recovered; failed access is not systematic absence.
Q: Which native CAV1 oligomer stoichiometries, alpha/beta ratios, modifications and cavin contacts occur in intact human caveolae, and how do they differ from bacterial detergent-purified 8S discs?
Q: Which purified membrane experiments separate direct bending by CAV1 from preferential residence in curved membranes, leaflet replacement and curvature effects of lipids or cavins?
Q: Which original mouse donor assays support the unresolved transcriptional, developmental, ciliary, metabolic, death-pathway and cardiac-electrophysiology transfers, and what source mapping supports the two lipid-droplet Reactome locations?
Q: Does the peptidase-activator transfer represent direct enhancement of enzyme chemistry or retention of MMP activity in a membrane compartment, given differing whole-tissue, raft and CAV1-peptide effects?
Q: Do the exact PAK1, EHD2-containing multi-partner and prostacyclin-synthase source experiments establish CAV1 interaction, rather than an affinity reagent, indirect complex association or a background review citation?
Q: How do native full-length human CAV1 and its two initiation products regulate eNOS versus other NOS isoforms, separately from the activities of isolated scaffolding-domain peptides?
Q: Which experiments connect the human lipodystrophy and PAH variants to specific coat/trafficking defects, and what additional evidence would resolve the limited dominant-lipodystrophy and ALS associations?
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Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)