Dynamin-1 is a large, predominantly neuronal GTPase that converts nucleotide hydrolysis into membrane remodeling during endocytosis. Its pleckstrin-homology domain binds phosphoinositides, its stalk supports self-assembly, and its proline-rich tail recruits SH3-domain partners. Assembly at membrane necks couples GTPase-domain interactions to constriction and vesicle scission, supporting receptor-mediated uptake and presynaptic membrane retrieval. Dynamin-1 also influences endocytic pit and vesicle dimensions. Alternative splicing changes an internal segment and the C-terminal tail; pathogenic variants can disrupt neuronal membrane trafficking and cause developmental and epileptic encephalopathy.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | KEEP AS NON CORE | Summary: UV-dependent mRNA capture provides limited positive RNA-binding evidence. Reason: The original author thesis Table S1 (PDF page 147) identifies DNM1 in class III: one experiment passes the study's threefold enrichment criterion, while the other two measurements are unavailable. Methods 3.5 uses UV crosslinking in HEK293 cells followed by denaturing oligo(dT) capture. This is positive screen evidence for RNA contact, rather than an inference from ordinary co-purification. Results 4.8 validates selected class I/II candidates; DNM1 was not tested individually, so its absence from that panel is not a failed validation. Limited replication and the unestablished physiological role justify non-core retention; neither proves the binding assertion exceeds the evidence. Supporting Evidence: |
| GO:0003924 GTPase activity | EXP PMID:15703209 SNX9 regulates dynamin assembly and is required for efficien... | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: Purified dynamin1 was assayed with SNX9; full-length SNX9 stimulated its GTP turnover, whereas the isolated SH3 domain bound without equivalent stimulation. The endogenous cell co-IP in that paper concerns DNM2 and is not needed for this catalytic conclusion. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Proposed replacements: membrane scission GTPase motor activity Supporting Evidence: |
| GO:0003924 GTPase activity | EXP PMID:8910402 Regulation of dynamin I GTPase activity by G protein betagam... | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: The cached original abstract directly reports stimulation and inhibition of dynamin1 GTP hydrolysis by phosphoinositide and G-protein beta-gamma subunits. Full assay text was not recovered; the chemical activity is independently established, so the experimental assertion is not challenged. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Proposed replacements: membrane scission GTPase motor activity Supporting Evidence: |
| GO:0003924 GTPase activity | EXP PMID:9362482 Domain structure and intramolecular regulation of dynamin GT... | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: The original abstract reports recombinant dynamin1 GTPase regulation and tetramerization. The recovered PMC page remains abstract-only. Independent human biochemical and structural work establishes the same catalytic machinery. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Proposed replacements: membrane scission GTPase motor activity Supporting Evidence: |
| GO:0003924 GTPase activity | IBA GO_REF:0000033 | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: The human PTN002480307 leaf descends from the asserted PTN000170013 node in PTHR11566. Its IBD has experimental descendants, including human DNM1 itself; that is legitimate target grounding, not circularity. No target loss of this catalytic function is evident. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000170013 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. Proposed replacements: membrane scission GTPase motor activity Supporting Evidence: GO_REF:0000033 |
| GO:0003924 GTPase activity | IDA PMID:20428113 G domain dimerization controls dynamin's assembly-stimulated... | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: The original human engineered GG construct joins residues 6–320 and 726–750. Transition-state G-domain dimerization explains assembly-stimulated hydrolysis, while independent reconstituted fission experiments establish the motor function of the intact target. The GG construct is not a natural splice product. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Proposed replacements: membrane scission GTPase motor activity |
| GO:0003924 GTPase activity | IEA GO_REF:0000120 | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: The source combines the dynamin GTPase-family InterPro assignments and RHEA:19669 chemistry with ARBA00026818. Official target domains and direct human experiments support hydrolysis. The ARBA condition branches include unresolved FunFam requirements, so an independently reconstructed complete rule match is not claimed. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: ARBA:ARBA00026818 UNRESOLVED The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. InterPro:IPR001401 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. InterPro:IPR003130 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. RHEA:19669 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. Proposed replacements: membrane scission GTPase motor activity Supporting Evidence: GO_REF:0000120 |
| GO:0003924 GTPase activity | TAS PMID:10944110 Dynamin mediates caveolar sequestration of muscarinic cholin... | MODIFY | Summary: Specify the membrane-scission GTPase motor activity. Reason: Human WT or K44A dynamin expressed in COS7 supplied cytosolic extracts for experiments with adult rat cardiac membranes. These support GTP-dependent endocytic sequestration; they are not purified human cardiomyocyte enzyme assays. Human fission and nucleotide-linked structural rotation justify the narrower GO:1990606 classification; its mechanochemical evidence and species limits are detailed in the source guide. This does not assign every mechanical measurement to this assay or every natural splice product. Proposed replacements: membrane scission GTPase motor activity Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10206341 Characterization of interactions of Nck with Sos and dynamin... | MODIFY | Summary: NCK1 association is mapped to its SH3 region. Reason: IntAct preserves a positive pull-down and co-IP for this literal human pair. Its separately annotated sufficient-binding region on NCK1 spans residues 182–260, encompassing the official third SH3 domain at 190–252. Together with the source abstract, this supports SH3-domain recognition rather than an invented adaptor function for DNM1. The parent-protein checksum does not identify the length of the binding reagent. Proposed replacements: SH3 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:10206341 Characterization of interactions of Nck with Sos and dynamin... | MODIFY | Summary: GRB2 binding is resolved to a demonstrated SH3 interface. Reason: The source-specific GRB2 pull-down is positive. Independent peptide-array/domain records and the 9922133 assembly-site study map DNM1 recognition to GRB2 SH3 domains. Refine this same partner claim on that combined evidence; no GRB2-like signaling-adaptor activity is assigned to DNM1. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:12791276 Auxilin-dynamin interactions link the uncoating ATPase chape... | KEEP AS NON CORE | Summary: Retain the purified Hsc70/auxilin associations with their mixed-species scope. Reason: The recovered original reports direct, nucleotide-dependent binding of dynamin1 to purified bovine Hsc70 and recombinant auxilin, including controls that distinguish independent binding from an unfolded chaperone substrate. This source row names both P19120 and Q27974. A single Hsp70-specific replacement would omit its auxilin component, and the assay does not make DNM1 a chaperone. The insect-cell dynamin reagent is not mapped to a current natural splice product. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:15252009 A novel dynamin-associating molecule, formin-binding protein... | MODIFY | Summary: FBP17 recognition requires its SH3 domain. Reason: The original Methods specifies human dynamin1 cDNA. Tagged FBP17 and its isolated SH3 fragment associate with DNM1; deleting the SH3 region or introducing P597L prevents association, with GST-domain pull-down corroboration. These domain-dependent experiments support the narrower term. They are not a purified full-length pair affinity measurement. Proposed replacements: SH3 domain binding Supporting Evidence: PMID:15252009 FBP17 interacts with dynamin |
| GO:0005515 protein binding | IPI PMID:15703209 SNX9 regulates dynamin assembly and is required for efficien... | MODIFY | Summary: Direct SNX9 SH3-domain binding is demonstrated. Reason: Purified full-length SNX9 and its SH3 domain bind recombinant dynamin1; deletion of the dynamin proline-rich domain or SNX9 SH3 region disrupts binding. Only full-length SNX9 efficiently stimulates assembly/GTPase activity. The binding term describes the experimentally mapped interface, not an adaptor activity of DNM1. Proposed replacements: SH3 domain binding Supporting Evidence: PMID:15703209 SNX9 binds directly to both dynamin-1 and dynamin-2. |
| GO:0005515 protein binding | IPI PMID:16234328 NOSTRIN functions as a homotrimeric adaptor protein facilita... | MODIFY | Summary: NOSTRIN recruits dynamin1 through its SH3 region. Reason: The original Methods explicitly identifies the human pcDNA-dynamin1 construct. Purified GST-NOSTRIN/SH3 baits recover DNM1 from transfected cell lysate, whereas the SH3 deletion does not; this mapping supports SH3-domain binding. The target was not purified in that pull-down, and the separate endogenous dynamin2 co-IP must not be relabeled as human DNM1 evidence. Proposed replacements: SH3 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:16432212 Nitric oxide regulates endocytosis by S-nitrosylation of dyn... | KEEP AS NON CORE | Summary: Retain the NOS3 association without inferring an enzyme-binding interface. Reason: Human HEK-cell reciprocal co-IP supports the literal NOS3/eNOS–DNM1 association and its nitric-oxide dependence. The purified DNM1 nitrosylation and GTPase experiments establish chemical regulation but do not measure purified NOS3–DNM1 contact. The bladder invasion experiments involving DNM2 remain a separate context. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17474147 Systematic identification of SH3 domain-mediated human prote... | MODIFY | Summary: A defined dynamin peptide binds the GRB2 SH3 domain. Reason: The exact IntAct peptide-array record identifies the GRB2 SH3 region 156–215 and the DNM1 sufficient-binding segment 780–792. This directly supports SH3-domain binding with a peptide-reagent limit; it does not establish full-length affinity or stoichiometry in cells. Parent accession/checksum fields are kept distinct from the separately annotated peptide features. Proposed replacements: SH3 domain binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17500595 Huntingtin interacting proteins are genetic modifiers of neu... | KEEP AS NON CORE | Summary: Retain the huntingtin-fragment binary interaction. Reason: The source used Htt residues 1–450 as bait in a sequence-confirmed and individually retested Y2H screen, with growth/reporter and background filters. The exact human DNM1–HTT records are positive. The separate mouse/human tissue AP-MS experiments are not pair-specific validation of this Y2H result, and no narrower partner-recognition activity is established. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:18353773 A novel sorting nexin modulates endocytic trafficking and al... | MODIFY | Summary: SNX33 association is dependent on its SH3 domain. Reason: The recovered original uses human cDNAs and shows DNM1 co-IP with SNX33 but not its SH3-deletion mutant, with unrelated protein controls (Figure 7A). The GST-SH3 experiment in Figure 7B principally pulls down endogenous DNM2 and is not a purified DNM1 assay. The target-specific deletion mapping nevertheless supports SH3-domain binding. Proposed replacements: SH3 domain binding Supporting Evidence: PMID:18353773 SNX33 bound the endocytic GTPase |
| GO:0005515 protein binding | IPI PMID:18353773 A novel sorting nexin modulates endocytic trafficking and al... | MODIFY | Summary: SNX9 association is consistent with its independently mapped SH3 contact. Reason: Figure 7A of the original explicitly includes human SNX9–DNM1 co-IP. Direct purified-domain and deletion experiments in 15703209 establish the narrower SH3 interface. The present paper does not independently measure that interface or assign every SNX33 perturbation result to SNX9. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:21706016 Selected reaction monitoring mass spectrometry reveals the d... | MODIFY | Summary: GRB2 complex capture is supported by independent SH3-interface evidence. Reason: The literal DNM1–GRB2 record is a positive tagged co-IP from HEK293T in the signaling study, not purified binding. Independent GRB2 SH3/defined-DNM1-peptide and assembly-site experiments justify the narrower target-level binding term. No source-specific stoichiometry or direct contact is inferred from the capture alone. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:21900206 A directed protein interaction network for investigating int... | KEEP AS NON CORE | Summary: Retain the DNM1–DNM2 association with the original screen limit explicit. Reason: The original describes full-length human bait/prey Y2H with individual retesting, but its exact DNM1–DNM2 supplementary record was not independently recovered. Multiple independent BioPlex, endogenous OpenCell and 40205054 primary AP-MS records positively support this same association. Retain the curated pair on the combined evidence, without claiming that the uninspected original row or a direct heterodimer interface was verified. |
| GO:0005515 protein binding | IPI PMID:24282027 Functional interaction of Parkinson's disease-associated LRR... | MODIFY | Summary: The LRRK2 interaction supports protein-kinase binding. Reason: The source tests a human LRRK2 N-terminal fragment in Y2H and independently confirms human full-length LRRK2–DNM1 co-IP; separate mouse dynamin constructs are labeled as such. LRRK2 is an experimentally established protein kinase. GO:0019901 describes binding to that protein class, not binding to its catalytic domain or DNM1-mediated kinase regulation. Proposed replacements: protein kinase binding Supporting Evidence: PMID:24282027 LRRK2 interacts with dynamin 1-3 |
| GO:0005515 protein binding | IPI PMID:29949766 Inhibition of Lysosome Membrane Recycling Causes Accumulatio... | KEEP AS NON CORE | Summary: Retain the SPG11 C-terminal interaction. Reason: Human DNM1 binds the SPG11 C-terminal bait 1943–2443 in Y2H, with a positive HeLa co-IP record. This supports association but does not establish that DNM1 directly executes lysosome reformation or ganglioside degradation. Dynasore inhibition is not target-specific evidence for all of those downstream processes. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:31980649 Extensive rewiring of the EGFR network in colorectal cancer ... | MODIFY | Summary: GRB2 capture corroborates a separately demonstrated SH3 interaction. Reason: Two exact DNM1–GRB2 records originate in tagged affinity purification from HCT116/HKE3 cells. The original quantitative affinity-capture measurements are complex associations. The SH3 refinement instead rests on independent defined-domain evidence for this same pair; no direct-contact inference is made from AP-MS. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | KEEP AS NON CORE | Summary: BioPlex supports a DNM1–DNM2 association. Reason: Exact positive records occur in HEK293T and HCT116 BioPlex contexts. The original uses tagged, sequence-verified ORFeome constructs and protein-group mass spectrometry. This supports co-complex association, not a purified heterodimer interface or an accession-resolved natural DNM1 splice product. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The GRB2 BioPlex hit is consistent with independent SH3 binding. Reason: The exact HEK293T AP-MS record is positive. Its complex-capture method does not identify an interface; the refinement is supported by the independent GRB2 SH3/defined-DNM1-peptide and assembly-site experiments for the same pair. Preserve the source assay limit and do not assign GRB2 signaling functions to DNM1. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The SNX33 association has independent SH3-dependent support. Reason: Two BioPlex records positively identify the literal DNM1–SNX33 pair. The SH3 refinement is grounded in the human deletion-controlled co-IP in 18353773, not in AP-MS alone. The available experiments do not determine a native purified-pair affinity. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: The SNX9 association has a directly established SH3 interface. Reason: The exact BioPlex pair is positive. Purified SNX9-domain/DNM1 experiments in 15703209 independently establish SH3 recognition, allowing refinement of the same target-level claim without reinterpreting AP-MS as direct binding. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:35271311 OpenCell: Endogenous tagging for the cartography of human ce... | KEEP AS NON CORE | Summary: Endogenous OpenCell proteomics supports DNM1–DNM2 association. Reason: The primary interaction CSV contains DNM1-bait/DNM2-prey row 7580 and the reciprocal gene-level row 7584. The first names reviewed DNM2 accessions; the reciprocal prey group lists unreviewed DNM1-related accessions, so it is not an accession-specific splice-product assay. Endogenous tagging, benzonase/digitonin extraction and affinity MS support association but not a purified interface. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:37871017 Spatacsin regulates directionality of lysosome trafficking b... | KEEP AS NON CORE | Summary: Retain the independently retested SPG11-fragment interaction. Reason: The exact positive Y2H record uses the human SPG11 C-terminal region 1943–2443 with an adult human brain library. The original distinguishes the exon32–34 deletion construct. This is positive binary fragment evidence; it does not by itself establish DNM1-driven directional lysosome transport or a specific partner-recognition class. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | KEEP AS NON CORE | Summary: The primary 2025 AP-MS graph verifies the DNM2–DNM1 pair. Reason: The paper-linked AP-MS network contains DNM2 bait node 568716, DNM1 prey node 560878 and edge 609892. This is a physical affinity-capture association, not a similarity embedding or an inferred shared assembly. The record does not specify a purified interface or current natural splice product. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MODIFY | Summary: The primary GRB2 AP-MS edge corroborates independent SH3 evidence. Reason: The primary graph contains GRB2 bait node 552668 to DNM1 prey node 560878, edge 568720. This verifies the literal association. The narrower SH3 claim comes from the independently mapped GRB2 interface, not the whole-map quality, shared embedding or AP-MS method alone. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | MODIFY | Summary: The primary SNX9 AP-MS edge corroborates direct domain binding. Reason: The primary graph contains SNX9 bait node 574484 to DNM1 prey node 560878, edge 605226. Purified-domain experiments in 15703209 provide independent evidence for SH3 recognition. No direct-contact or isoform claim is assigned to this graph edge itself. Proposed replacements: SH3 domain binding |
| GO:0005515 protein binding | IPI PMID:9922133 Dual function C-terminal domain of dynamin-1: modulation of ... | MODIFY | Summary: The GRB2 interaction maps to SH3 recognition of the proline-rich tail. Reason: The original abstract describes binding of SH3-domain proteins to the dynamin1 C-terminal assembly region, with different assembly effects for fragments and intact protein. The full original was not recovered; the exact peptide-array record in 17474147 independently corroborates the defined interface. Refine the binding activity without equating fragment inhibition with a universal physiological effect. Proposed replacements: SH3 domain binding |
| GO:0005525 GTP binding | IEA GO_REF:0000002 | ACCEPT | Summary: GTP binding is an integral part of the catalytic motor. Reason: The target InterPro GTPase-family assignments are consistent with the official nucleotide-binding features and direct human nucleotide-bound structures. Retain the substrate-binding assertion as part of the integrated motor mechanism, not as an independent core activity. Propagation Review Root cause: NO FAILURE CORE Sources checked: InterPro:IPR001401 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. InterPro:IPR003130 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. InterPro:IPR030381 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. |
| GO:0005546 phosphatidylinositol-4,5-bisphosphate binding | IDA PMID:9765310 The pleckstrin homology domains of dynamin isoforms require ... | ACCEPT | Summary: Phosphatidylinositol-4,5-bisphosphate binding anchors the motor to membranes. Reason: The original abstract reports oligomerization-dependent phosphoinositide binding by dynamin PH-domain constructs. Independent human dynamin1 liposome and PIP2-binding assays corroborate this lipid-recognition mechanism. The abstract-only access is explicit; no unobserved binding constant or all-isoform specificity is asserted. |
| GO:0005546 phosphatidylinositol-4,5-bisphosphate binding | IMP PMID:10074457 Dominant-negative inhibition of receptor-mediated endocytosi... | ACCEPT | Summary: PH-domain perturbation supports functional PIP2 recognition. Reason: The original abstract connects PH-domain changes to phosphoinositide binding and endocytic defects. Human biochemical and structural evidence independently supports PIP2-dependent membrane recruitment. Retain the experimental assertion without replacing its source identity or inventing unavailable figure details. |
| GO:0005547 phosphatidylinositol-3,4,5-trisphosphate binding | IDA PMID:9765310 The pleckstrin homology domains of dynamin isoforms require ... | KEEP AS NON CORE | Summary: Retain measured PIP3 recognition as a broader lipid-binding capacity. Reason: The source abstract reports phosphoinositide recognition by oligomerized PH-domain reagents, and the official target domain description includes PIP3. This positive binding capacity is retained, while a distinct PIP3-dependent physiological motor pathway is not established by the available evidence. Supporting Evidence: |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the conserved cytoplasmic pool. Reason: The human leaf descends from the cytoplasm IBD node PTN000170013. Cytoplasmic soluble/particulate pools and transient recruitment to endocytic sites are compatible with the source. The broad compartment is retained non-core alongside the precise functional pit location; it is not replaced by a cross-branch plasma-membrane term or treated as evidence of exclusively free solubility. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000170013 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. |
| GO:0005874 microtubule | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain conserved microtubule association outside the principal membrane-scission core. Reason: The valid PTN000170013 placement includes experimentally grounded plant, nematode and mammalian descendants. The source is a phylogenetic assertion, not a demand for a new human localization experiment. The microtubule-associated pool is compatible with the official target summary but is not equated with an independently established human microtubule motor core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000170013 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. Supporting Evidence: GO_REF:0000033 |
| GO:0005886 plasma membrane | EXP PMID:15703209 SNX9 regulates dynamin assembly and is required for efficien... | ACCEPT | Summary: Plasma-membrane recruitment is central to endocytic scission. Reason: The original images tagged dynamin1 recruitment to surface endocytic structures; endogenous SNX9 co-IP with DNM2 is a separate experiment. This is a peripheral, dynamic membrane association, not a claim that DNM1 is an integral transmembrane protein or permanently confined to this compartment. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Plasma-membrane recruitment is central to endocytic scission. Reason: The human leaf descends from the plasma-membrane node PTN008520579; no target-specific loss is evident. This is a peripheral, dynamic membrane association, not a claim that DNM1 is an integral transmembrane protein or permanently confined to this compartment. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN008520579 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Plasma-membrane recruitment is central to endocytic scission. Reason: The official UniProt subcellular-location mapping SL-0039 explicitly supplies the plasma-membrane assertion. This is a peripheral, dynamic membrane association, not a claim that DNM1 is an integral transmembrane protein or permanently confined to this compartment. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0039 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. |
| GO:0005886 plasma membrane | TAS Reactome:R-HSA-3928654 | ACCEPT | Summary: Plasma-membrane recruitment is central to endocytic scission. Reason: The saved Reactome path is reaction 3928654 input to physical entity 177488, explicitly human UniProt Q05193 residues 1–864 at the plasma membrane. It is not inferred from an unspecified family member. This is a peripheral, dynamic membrane association, not a claim that DNM1 is an integral transmembrane protein or permanently confined to this compartment. |
| GO:0005905 clathrin-coated pit | IDA PMID:8101525 Mutations in human dynamin block an intermediate stage in co... | ACCEPT | Summary: Clathrin-coated pits are a principal functional site. Reason: The human mutant study places dynamin at the coated-vesicle formation stage, and independent recruitment and membrane-remodeling experiments substantiate this location. The original 8101525 cache and recovered scanned XML are abstract-only; the curator-backed location is retained using the independent positive target evidence. |
| GO:0005905 clathrin-coated pit | IEA GO_REF:0000044 | ACCEPT | Summary: Clathrin-coated pits are a principal functional site. Reason: The human mutant study places dynamin at the coated-vesicle formation stage, and independent recruitment and membrane-remodeling experiments substantiate this location. The source SL-0069 mapping is consistent with the official target location and independent experiments. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0069 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. |
| GO:0006897 endocytosis | IMP PMID:19706678 Axonal targeting of Caspr2 in hippocampal neurons via select... | TOO GENERAL | Summary: Endocytosis is retained through its more informative receptor-mediated descendant. Reason: The original uses GFP-Dynamin1 WT/K44A in embryonic-day18 rat hippocampal neurons. K44A blocks Caspr2 internalization and reduces EEA1-positive vesicles. Human DNM1 biochemical fission establishes the performed step independently, so this is not merely a downstream disease association. The host neurons are rat and the methods cite the historical construct without resolving a current splice accession. The broad term is true, but GO:0006898 receptor-mediated endocytosis is an asserted strict descendant that already captures the endocytic role at this level. TOO_GENERAL concerns redundant term coverage, not the validity or species scope of this experiment. |
| GO:0006897 endocytosis | TAS PMID:16648839 GTP-dependent twisting of dynamin implicates constriction an... | TOO GENERAL | Summary: Endocytosis is retained through its more informative receptor-mediated descendant. Reason: The original supplementary Methods uses rat-brain dynamin purified with an SH3 affinity reagent and reports confirmation of selected experiments with purified human dynamin1 from baculovirus. Its detailed tube/vesicle measurements support endocytic mechanics, but unspecified selected confirmations cannot be relabeled as every assay being human or as identifying a natural isoform. The broad term is true, but GO:0006898 receptor-mediated endocytosis is an asserted strict descendant that already captures the endocytic role at this level. TOO_GENERAL concerns redundant term coverage, not the validity or species scope of this experiment. |
| GO:0006898 receptor-mediated endocytosis | IDA PMID:8101525 Mutations in human dynamin block an intermediate stage in co... | ACCEPT | Summary: Retain receptor-mediated endocytosis as an executed cellular role. Reason: The historical human mutant study directly concerns coated-vesicle formation; available abstract evidence is consistent with independent human endocytic perturbation work. DNM1 supplies membrane-remodeling/scission work rather than being merely cargo consumed by endocytosis. |
| GO:0006898 receptor-mediated endocytosis | IEA GO_REF:0000117 | ACCEPT | Summary: Retain receptor-mediated endocytosis as an executed cellular role. Reason: ARBA00044584 and the official record support this process. FunFam-dependent rule branches are not independently proven to fire, but direct experimental target evidence substantiates the biological assertion. DNM1 supplies membrane-remodeling/scission work rather than being merely cargo consumed by endocytosis. Propagation Review Root cause: NO FAILURE CORE Sources checked: ARBA:ARBA00044584 UNRESOLVED The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. |
| GO:0006898 receptor-mediated endocytosis | IMP PMID:10074457 Dominant-negative inhibition of receptor-mediated endocytosi... | ACCEPT | Summary: Retain receptor-mediated endocytosis as an executed cellular role. Reason: The source uses dynamin PH-domain perturbations to connect membrane binding to receptor-mediated uptake; the abstract is available, and independent human experiments corroborate the claim. DNM1 supplies membrane-remodeling/scission work rather than being merely cargo consumed by endocytosis. |
| GO:0006898 receptor-mediated endocytosis | IMP PMID:10521508 Trafficking of the HIV coreceptor CXCR4. Role of arrestins a... | ACCEPT | Summary: Retain receptor-mediated endocytosis as an executed cellular role. Reason: The cached abstract reports that dominant-negative dynamin-1 and arrestin-3 inhibit PMA- and SDF-1alpha-induced CXCR4 internalization in transfected COS-1 and HEK-293 cells. Full Methods were not recovered, so the dynamin mutant identity and natural splice product are not assigned. This positive receptor-internalization result supports the curated process; independent biochemical evidence establishes that DNM1 supplies membrane-remodeling/scission work rather than being merely cargo consumed by endocytosis. |
| GO:0007032 endosome organization | IMP PMID:19706678 Axonal targeting of Caspr2 in hippocampal neurons via select... | KEEP AS NON CORE | Summary: Retain the experimentally supported endosome-organization context. Reason: In the actual rat-neuron experiment, GFP-Dynamin1 K44A prevents formation of the EEA1-positive early-endosome pattern while WT permits Caspr2 delivery. This supports the curated organization phenotype, with a dominant-negative and upstream-membrane-traffic interpretation. It does not establish a second independent endosome-building molecular activity. Supporting Evidence: |
| GO:0008017 microtubule binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain inherited microtubule-binding capacity. Reason: The human leaf inherits the valid PTN000170013 IBD. The fly shibire donor P27619 has an experimental IDA annotation to 11076973; the recovered source identifies dynamin among proteins enriched in microtubule cosedimentation experiments. A single experimental donor is not weak phylogenetic evidence. This association remains outside the established membrane-scission core, without claiming a purified human affinity measurement. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000170013 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. |
| GO:0016020 membrane | IEA GO_REF:0000117 | MODIFY | Summary: Specify the established plasma-membrane association. Reason: The generic membrane assertion is supported, but the principal target-level compartment can be stated as plasma membrane using direct recruitment and the exact Reactome Q05193 entity. ARBA00028763 has unresolved FunFam conditions in the reconstruction, so this is a biological refinement supported independently, not a claim to have proven a complete electronic rule match or excluded other membrane pools. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: ARBA:ARBA00028763 UNRESOLVED The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. Proposed replacements: plasma membrane |
| GO:0016185 synaptic vesicle budding from presynaptic endocytic zone membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Inherited presynaptic vesicle budding fits the membrane-scission mechanism. Reason: The human leaf descends from PTN000902093; the fly shibire donor has a curated experimental budding annotation, with temperature-sensitive depletion of synaptic vesicles explicitly described in 15014125. Mouse hippocampal loss of Dnm1 also impairs retrieval, and human DNM1 rescues the measured endocytic fluorescence response. This supports conserved participation without transferring fly calcium-buffering conclusions to DNM1. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000902093 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. |
| GO:0019003 GDP binding | ISS GO_REF:0000024 | ACCEPT | Summary: GDP binding is directly compatible with the catalytic cycle. Reason: The ISS donor P39053 carries the same GDP-binding assertion. Human dynamin1 G-domain nucleotide complexes directly corroborate the product-bound state. The donor record cites 20428113, whose engineered catalytic construct is human; it must not be described as a mouse-specific GDP experiment. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P39053 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. |
| GO:0019901 protein kinase binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain kinase association without making it a separate core. Reason: The mouse donor P39053 has a curated LRRK2 interaction grounded in 21307259, whose original uses adult mouse-brain domain pull-down proteomics. Independent human LRRK2–DNM1 binary-fragment and full-length co-IP evidence in 24282027 substantiates the target-level protein-kinase-binding claim. Neither source establishes that DNM1 modulates the kinase catalytic site. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P39053 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. |
| GO:0030139 endocytic vesicle | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain transient association with endocytic vesicular structures. Reason: The rat P21575 donor is experimentally annotated from 17257598. Its recovered original distinguishes purified rat-brain dynamin, human transfected DNM1 binding controls, and RFP-Dynamin1 in Swiss3T3 endocytic puncta. These support the conserved transient compartment; not every punctum is a mature detached vesicle or an accession-resolved human product. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P21575 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000044 | MODIFY | Summary: Resolve the broad vesicle category to endocytic vesicles. Reason: The source is the official SL-0088 cytoplasmic-vesicle mapping. The refinement uses the target mechanism and donor-specific compartment evidence, not a claim that every cytoplasmic vesicle contains DNM1 or that the original broad assay itself resolved vesicle identity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB-SubCell:SL-0088 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. Proposed replacements: endocytic vesicle |
| GO:0031410 cytoplasmic vesicle | ISS GO_REF:0000024 | MODIFY | Summary: Resolve the broad vesicle category to endocytic vesicles. Reason: The source transfers from rat P21575, whose endocytic structures are experimentally supported in 17257598. The refinement uses the target mechanism and donor-specific compartment evidence, not a claim that every cytoplasmic vesicle contains DNM1 or that the original broad assay itself resolved vesicle identity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P21575 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. Proposed replacements: endocytic vesicle |
| GO:0031410 cytoplasmic vesicle | ISS GO_REF:0000024 | MODIFY | Summary: Resolve the broad vesicle category to endocytic vesicles. Reason: The source transfers from mouse P39053. Its 19781630 donor publication remains abstract-only, so its exact localization experiment is not reconstructed; independent direct target and rodent data establish the more specific conserved endocytic compartment. The refinement uses the target mechanism and donor-specific compartment evidence, not a claim that every cytoplasmic vesicle contains DNM1 or that the original broad assay itself resolved vesicle identity. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: UniProtKB:P39053 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. Proposed replacements: endocytic vesicle |
| GO:0042583 chromaffin granule | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Retain the specialized chromaffin-granule association. Reason: The source maps official SL-0061 to the specialized chromaffin secretory vesicle. The official record places the associated rapid-endocytosis context in conserved chromaffin biology. This is a contextual vesicle pool, not evidence that DNM1 synthesizes or stores catecholamines, and is retained outside the principal neuronal/clathrin-pit core. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB-SubCell:SL-0061 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. Supporting Evidence: GO_REF:0000044 |
| GO:0042802 identical protein binding | IPI PMID:20428113 G domain dimerization controls dynamin's assembly-stimulated... | MODIFY | Summary: Specify the directly measured homodimerization interface. Reason: The human engineered GG construct forms the nucleotide-dependent G-domain dimer that stimulates hydrolysis. This supports homodimerization rather than only generic identical-protein binding. The engineered fragment is not a natural isoform and does not imply that every full-length assembly is a dimer. Proposed replacements: protein homodimerization activity Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:20700106 Dynamin GTPase regulation is altered by PH domain mutations ... | KEEP AS NON CORE | Summary: Retain human dynamin1 self-association in several assembly states. Reason: The original explicitly uses human dynamin1 ba and distinguishes full-length tetramers from engineered delta-PRD/R399A/I690K dimers in SAXS and related assays. The broad self-association claim is sound but does not represent a separate function beyond the integrated assembly-coupled motor. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:21927000 Crystal structure of nucleotide-free dynamin. | KEEP AS NON CORE | Summary: Retain direct structural and solution self-association evidence. Reason: The genuine supplementary captions describe human dynamin1 delta-PRD purification and solution populations extending from dimers to larger oligomers, with engineered IHGIR/K562E variants altering the distribution. Preserve broad self-association; do not label the engineered structure as a specific natural splice product. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:21962517 A pseudoatomic model of the dynamin polymer identifies a hyd... | KEEP AS NON CORE | Summary: Retain self-association supported by crosslinking and assembly assays. Reason: The original studies full-length R15C/R730C engineered dynamin and distinguishes MTS crosslinked dimers from BS3-linked tetramers, with gel filtration/proteolytic controls and polymer reconstruction. These support the identical-protein interaction without creating an independent oligomerization core or extrapolating one stoichiometry to every condition. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:26302298 Crystal structure of the dynamin tetramer. | KEEP AS NON CORE | Summary: The dynamin3 headline does not invalidate actual human dynamin1 controls. Reason: The recovered original and Extended Data Figure 2 explicitly include human dynamin1 delta-PRD controls: R361S/R399A behaves as a dimer, whereas I481D/H687D/L688S yields a monomeric control. Thus the target self-association is supported. The main tetramer crystal is dynamin3 and is not misrepresented as a human DNM1 natural-product structure. Supporting Evidence: |
| GO:0042802 identical protein binding | IPI PMID:30069048 Cryo-EM of the dynamin polymer assembled on lipid membrane. | KEEP AS NON CORE | Summary: Retain polymer self-association within the integrated motor mechanism. Reason: The original human delta-PRD cryo-EM polymer and separately tested full-length cellular constructs demonstrate assembly. These are not independent evidence for every natural splice product, and polymer association does not by itself specify only homodimer binding. The figure-label correction changes neither this conclusion nor the publication validity. |
| GO:0042803 protein homodimerization activity | IDA PMID:20428113 G domain dimerization controls dynamin's assembly-stimulated... | ACCEPT | Summary: G-domain homodimerization is an experimentally established motor mechanism. Reason: The human engineered catalytic construct directly demonstrates transition-state dimerization and its coupling to stimulated GTP hydrolysis. Retain this mechanistic binding activity within the single motor core rather than proposing a second unrelated core. Supporting Evidence: |
| GO:0045202 synapse | IBA GO_REF:0000033 | MODIFY | Summary: Specify the presynaptic compartment of the conserved synaptic role. Reason: The human leaf descends from the synapse IBD node PTN000902093. The actual rat source shows dynamin1 immunoreactivity at nerve terminals, and mouse neuronal endocytosis experiments support the same compartment. Presynapse is a verified ontology descendant of synapse; this target-level refinement does not claim the original PAINT node explicitly encoded the narrower term. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000902093 SUPPORTS TRANSFER Exact IBD and target descent verified in PTHR11566. Experimental descendant evidence is positive; the target appearing among the seeds is legitimate grounding. Proposed replacements: presynapse |
| GO:0051260 protein homooligomerization | IDA PMID:9765310 The pleckstrin homology domains of dynamin isoforms require ... | ACCEPT | Summary: Homooligomerization supplies the membrane-remodeling assembly. Reason: The original PH-domain study connects multimerization to phosphoinositide affinity. Independent purified/structural human studies demonstrate assembly into higher oligomers. The annotation describes a performed self-assembly step of the motor, not an added independent biological program. |
| GO:0051289 protein homotetramerization | IDA PMID:9362482 Domain structure and intramolecular regulation of dynamin GT... | ACCEPT | Summary: Tetramerization is one directly supported solution assembly state. Reason: The original abstract reports a recombinant dynamin1 tetramer, with independent human solution evidence in 20700106. Retain this experimentally supported state without implying a fixed tetramer at every membrane neck or throughout GTP turnover. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | UNDECIDED | Summary: The source-specific extracellular-vesicle identification remains unresolved. Reason: The genuine original describes EPS-urine differential ultracentrifugation and Q-Exactive proteomics, with the target protein list in Supplementary Table 2. The attempted workbook and EPMC supplement routes returned challenge/not-open-access payloads, so the DNM1 identification and peptide grouping could not be inspected. Do not remove the curator-backed assertion or infer contamination from a predominantly intracellular function; retain it as undecided pending the actual target record. Supporting Evidence: |
| GO:0097494 regulation of vesicle size | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the conserved pre-fission vesicle-size regulatory context. Reason: The mouse donor P39053 is experimentally grounded in 35220002: Dnm1 loss increases vesicle diameters and produces larger membrane pits. The human DNM1 rescue in that paper restores endocytic fluorescence kinetics, not a reported EM vesicle-size endpoint. The conserved size-control assertion is retained with that distinction; its precise molecular linkage to coat assembly versus scission remains unresolved. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:P39053 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. |
| GO:0098793 presynapse | IEA GO_REF:0000044 | ACCEPT | Summary: Presynaptic enrichment supports synaptic vesicle retrieval. Reason: The official SL-0516 location mapping is consistent with directly observed dynamin1 nerve-terminal localization in the recovered rat original and the established neuronal membrane-retrieval role. This is a conserved compartment claim, not an assertion of identical expression across all human splice products. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB-SubCell:SL-0516 SUPPORTS TRANSFER The asserted mapping is retained. Exact source/domain or subcellular-location scope is discussed above; unresolved FunFam conditions are not treated as proven rule execution. |
| GO:0098793 presynapse | ISS GO_REF:0000024 | ACCEPT | Summary: Presynaptic enrichment supports synaptic vesicle retrieval. Reason: The rat P21575 ISS donor is consistent with directly observed dynamin1 nerve-terminal localization in the recovered rat original and the established neuronal membrane-retrieval role. This is a conserved compartment claim, not an assertion of identical expression across all human splice products. Propagation Review Root cause: NO FAILURE CORE Sources checked: UniProtKB:P21575 SUPPORTS TRANSFER Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. |
| GO:0099049 clathrin coat assembly involved in endocytosis | ISS GO_REF:0000024 | UNDECIDED | Summary: Specific clathrin-cage assembly is not resolved by the donor measurements. Reason: The mouse P39053 source is annotated to 35220002. That original measures endocytic fluorescence, vesicle/pit dimensions and clathrin abundance; its coat-maturation discussion cites prior work. GO:0099049 specifically describes assembly of clathrin triskelia into a cage. The data support an upstream role in pit formation and size but do not resolve whether DNM1 itself performs or regulates that precise assembly step. Leave the inherited assertion undecided rather than calling the measured size phenotype a direct coat-assembly assay or rejecting a possible role. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P39053 UNRESOLVED Actual donor identity and current source annotation were inspected; the review distinguishes donor assay, human corroboration and remaining source limits. |
| GO:0099050 vesicle scission | IDA PMID:19084269 GTPase cycle of dynamin is coupled to membrane squeeze and r... | ACCEPT | Summary: GTP-dependent membrane severing is the defining directly measured activity. Reason: The original reconstitutes non-leaky nanotube closure/fission with dynamin and distinguishes hydrolyzable GTP from GTPgammaS controls. The cited purification protocol identifies human dynamin1 cDNA, but does not resolve a current natural splice product. DNM1 performs the membrane-remodeling work rather than being cargo required for the process. |
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Q: Does DNM1 directly participate in clathrin cage assembly, or does its pre-fission effect on pit dimensions arise through other membrane-remodeling or recruitment steps?
Q: Can the DNM1 peptide/protein-group entry in the EPS-urine extracellular-vesicle dataset be recovered and independently verified?
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