GABARAP (gamma-aminobutyric acid receptor-associated protein) is a ubiquitin-like protein of the Atg8 family (GABARAP subfamily). Like other Atg8 proteins it is processed by ATG4 to expose a C-terminal glycine (Gly116) and is conjugated by ATG7, ATG3 and the ATG12-ATG5-ATG16L1 complex to phosphatidylethanolamine on phagophore and autophagosome membranes (form II). Its hydrophobic LIR-docking site binds LC3-interacting region motifs, with a preference for GABARAP-interaction motifs, in autophagy receptors and effectors. GABARAP-subfamily proteins contribute to autophagosome formation and are the main Atg8 proteins for autophagosome-lysosome fusion, where they recruit PLEKHM1, and for PINK1/Parkin mitophagy; GABARAP also binds ER-phagy receptors such as UBAC2 and TEX264. On conjugated endolysosomal and autophagic membranes it sequesters the FLCN-FNIP complex through an LIR in FNIP, blocking RagC/D activation and so allowing TFEB/TFE3 nuclear entry and lysosome biogenesis. GABARAP was first identified as a binding partner of the GABA(A) receptor gamma2 subunit that also binds tubulin and is linked to receptor trafficking in neurons; it additionally scaffolds the CUL3-KBTBD6/7 ubiquitin ligase on membranes to degrade the RAC1 activator TIAM1.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000045 autophagosome assembly | IBA GO_REF:0000033 | ACCEPT | Summary: GABARAP-subfamily proteins on the phagophore contribute to autophagosome biogenesis. Reason: Atg8-family proteins promote efficient autophagosome formation (loss of all six gives smaller, slower-forming autophagosomes). GABARAP mainly acts at later steps, but its participation in assembly at the membrane is supported and consistent with the IBA. Supporting Evidence: PMID:27864321 loss of all Atg8s yields smaller autophagosomes and a slowed initial rate of autophagosome formation PMID:20418806 our results indicate that LC3s are involved in elongation of the phagophore membrane whereas the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation |
| GO:0000139 Golgi membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: A pool of GABARAP is associated with Golgi membranes, particularly in neurons. Reason: Transferred from rat/mouse GABARAP; consistent with the Golgi-associated pool implicated in GABA(A) receptor trafficking, which is a secondary function. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae |
| GO:0000139 Golgi membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: A pool of GABARAP is associated with Golgi membranes, particularly in neurons. Reason: Transferred from rat/mouse GABARAP; consistent with the Golgi-associated pool implicated in GABA(A) receptor trafficking, which is a secondary function. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae |
| GO:0000421 autophagosome membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Lipidated GABARAP (form II) is associated with autophagosomal membranes. Reason: Shown directly for GABARAP form II and conserved across Atg8-family proteins. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. PMID:15169837 These results suggest that all mammalian Atg8 homologues receive a common modification to associate with autophagosomal membrane as the form II. |
| GO:0000421 autophagosome membrane | IDA PMID:15169837 LC3, GABARAP and GATE16 localize to autophagosomal membrane ... | ACCEPT | Summary: Lipidated GABARAP (form II) is associated with autophagosomal membranes. Reason: Shown directly for GABARAP form II and conserved across Atg8-family proteins. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. PMID:15169837 These results suggest that all mammalian Atg8 homologues receive a common modification to associate with autophagosomal membrane as the form II. |
| GO:0000421 autophagosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Lipidated GABARAP (form II) is associated with autophagosomal membranes. Reason: Shown directly for GABARAP form II and conserved across Atg8-family proteins. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. |
| GO:0000421 autophagosome membrane | TAS Reactome:R-HSA-5682388 | ACCEPT | Summary: Lipidated GABARAP (form II) is associated with autophagosomal membranes. Reason: Shown directly for GABARAP form II and conserved across Atg8-family proteins. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. |
| GO:0000421 autophagosome membrane | TAS Reactome:R-HSA-8854588 | ACCEPT | Summary: Lipidated GABARAP (form II) is associated with autophagosomal membranes. Reason: Shown directly for GABARAP form II and conserved across Atg8-family proteins. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. |
| GO:0000423 mitophagy | IBA GO_REF:0000033 | ACCEPT | Summary: GABARAP-subfamily proteins are the main Atg8 contributors to PINK1/Parkin mitophagy. Reason: Knockout analysis identifies GABARAP subfamily members as primary contributors to PINK1/Parkin mitophagy; consistent with the IBA. Supporting Evidence: PMID:27864321 identify GABARAP subfamily members as primary contributors to PINK1/Parkin mitophagy and starvation autophagy |
| GO:0005515 protein binding | IPI PMID:11096062 The human homolog of Saccharomyces cerevisiae Apg7p is a Pro... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:11146101 Interaction of the Unc-51-like kinase and microtubule-associ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:15977068 GABAA receptor-associated protein (GABARAP) induces apoptosi... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:16169070 A human protein-protein interaction network: a resource for ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:16303767 Phosphatidylserine in addition to phosphatidylethanolamine i... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:16303767 Phosphatidylserine in addition to phosphatidylethanolamine i... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:17580304 p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19056683 The TP53INP2 protein is required for autophagy in mammalian ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19154346 Structural framework of the GABARAP-calreticulin interface--... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19250911 A role for NBR1 in autophagosomal degradation of ubiquitinat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:19250911 A role for NBR1 in autophagosomal degradation of ubiquitinat... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20010802 Nix is a selective autophagy receptor for mitochondrial clea... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20200478 Nix, a receptor protein for mitophagy in mammals. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20200478 Nix, a receptor protein for mitophagy in mammals. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20452972 p62/SQSTM1 is a target gene for transcription factor NRF2 an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20562859 Network organization of the human autophagy system. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:20810658 Starch binding domain-containing protein 1/genethonin 1 is a... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:21617041 Phosphorylation of the autophagy receptor optineurin restric... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:22267086 Mitochondrial outer-membrane protein FUNDC1 mediates hypoxia... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:22354992 Rab GTPase-activating proteins in autophagy: regulation of e... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:22421968 TP53INP1, a tumor suppressor, interacts with LC3 and ATG8-fa... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:22470510 DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:22470510 DOR/Tp53inp2 and Tp53inp1 constitute a metazoan gene family ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:22948227 MAPK15/ERK8 stimulates autophagy by interacting with LC3 and... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24089205 Autophagy promotes primary ciliogenesis by removing OFD1 fro... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24089205 Autophagy promotes primary ciliogenesis by removing OFD1 fro... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24290141 Structural basis of the autophagy-related LC3/Atg13 LIR comp... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:24879152 Phosphorylation of NBR1 by GSK3 modulates protein aggregatio... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25126726 FLCN, a novel autophagy component, interacts with GABARAP an... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25500191 PLEKHM1 regulates Salmonella-containing vacuole biogenesis a... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:26040720 Regulation of endoplasmic reticulum turnover by selective au... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:26347139 TRIM-mediated precision autophagy targets cytoplasmic regula... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:26347139 TRIM-mediated precision autophagy targets cytoplasmic regula... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:28712572 Centriolar Satellites Control GABARAP Ubiquitination and GAB... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:28712572 Centriolar Satellites Control GABARAP Ubiquitination and GAB... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:31006538 Intrinsically Disordered Protein TEX264 Mediates ER-phagy. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:31006538 Intrinsically Disordered Protein TEX264 Mediates ER-phagy. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:31006538 Intrinsically Disordered Protein TEX264 Mediates ER-phagy. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:31006538 Intrinsically Disordered Protein TEX264 Mediates ER-phagy. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:32315611 A DNM2 Centronuclear Myopathy Mutation Reveals a Link betwee... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33436498 Cytoplasmic short linear motifs in ACE2 and integrin Ξ²(3) li... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33452816 The endolysosomal adaptor PLEKHM1 is a direct target for bot... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:34597140 GABARAP sequesters the FLCN-FNIP tumor suppressor complex to... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:34597140 GABARAP sequesters the FLCN-FNIP tumor suppressor complex to... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:36481789 Deficiency of cancer/testis antigen gene CT55 causes male in... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:37219487 Large-scale phosphomimetic screening identifies phospho-modu... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:37219487 Large-scale phosphomimetic screening identifies phospho-modu... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:37252361 Semisynthetic LC3 Probes for Autophagy Pathways Reveal a Non... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:39284914 ER-phagy restrains inflammatory responses through its recept... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005515 protein binding | IPI PMID:9892355 GABA(A)-receptor-associated protein links GABA(A) receptors ... | REMOVE | Summary: The reported interaction is retained as evidence, but generic protein binding is uninformative. Reason: The cited interaction evidence can inform complex membership, LIR-mediated recruitment or a demonstrated regulatory/adaptor mechanism. Generic protein binding does not identify that function; removing this annotation does not reject the measured interaction or assign an untested mechanism to every interactor. |
| GO:0005543 phospholipid binding | IEA GO_REF:0000117 | ACCEPT | Summary: GABARAP is covalently conjugated to phosphatidylethanolamine via its C-terminal glycine. Reason: Broad parent of phosphatidylethanolamine binding; correct but less specific. Supporting Evidence: PMID:15169837 two other mammalian homologues of yeast Atg8, gamma-aminobutyric-acid-type-A-receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE16) also generate form II, which are recovered in membrane fractions |
| GO:0005764 lysosome | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Lipidated GABARAP is present on autolysosomes and on endolysosomal membranes during conjugation of ATG8 to single membranes. Reason: Transferred from mouse. GABARAP is delivered to lysosomes with autophagosomes and is conjugated to endolysosomal membranes under CASM, but lysosome is not a resident location. Supporting Evidence: PMID:34597140 the membrane conjugation of GABARAP, but not LC3, is required for activation of TFEB/TFE3 to control lysosomal capacity |
| GO:0005776 autophagosome | IDA PMID:19056683 The TP53INP2 protein is required for autophagy in mammalian ... | ACCEPT | Summary: GABARAP is a component of autophagosomes. Reason: Well established for the lipidated form; the cited study shows TP53INP2 recruiting LC3/GABARAP proteins to autophagosome membranes. Supporting Evidence: PMID:19056683 TP53INP2 is a scaffold protein that recruits LC3 and/or LC3-related proteins to the autophagosome membrane |
| GO:0005776 autophagosome | IEA GO_REF:0000117 | ACCEPT | Summary: GABARAP is a component of autophagosomes. Reason: Well established for the lipidated form; the cited study shows TP53INP2 recruiting LC3/GABARAP proteins to autophagosome membranes. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. |
| GO:0005790 smooth endoplasmic reticulum | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Transferred from mouse GABARAP localization data. Reason: Association with intracellular (including ER-derived) membranes is plausible for an Atg8-family protein, but smooth ER is not an established functional location of human GABARAP. |
| GO:0005794 Golgi apparatus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: A pool of GABARAP is associated with Golgi membranes, particularly in neurons. Reason: Transferred from rat/mouse GABARAP; consistent with the Golgi-associated pool implicated in GABA(A) receptor trafficking, which is a secondary function. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5678490 | ACCEPT | Summary: Unconjugated GABARAP (form I) is cytosolic before lipidation. Reason: Correct; the cytosolic pool is the substrate of the Atg8 conjugation reactions represented in Reactome. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5681987 | ACCEPT | Summary: Unconjugated GABARAP (form I) is cytosolic before lipidation. Reason: Correct; the cytosolic pool is the substrate of the Atg8 conjugation reactions represented in Reactome. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5682011 | ACCEPT | Summary: Unconjugated GABARAP (form I) is cytosolic before lipidation. Reason: Correct; the cytosolic pool is the substrate of the Atg8 conjugation reactions represented in Reactome. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5682377 | ACCEPT | Summary: Unconjugated GABARAP (form I) is cytosolic before lipidation. Reason: Correct; the cytosolic pool is the substrate of the Atg8 conjugation reactions represented in Reactome. |
| GO:0005829 cytosol | TAS Reactome:R-HSA-5682388 | ACCEPT | Summary: Unconjugated GABARAP (form I) is cytosolic before lipidation. Reason: Correct; the cytosolic pool is the substrate of the Atg8 conjugation reactions represented in Reactome. |
| GO:0005856 cytoskeleton | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: GABARAP binds tubulin and colocalizes with microtubules. Reason: Cytoskeletal association is linked to its role in GABA(A) receptor trafficking and is not part of its core autophagy function. Actin cytoskeleton association is weakly supported. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Colocalizes with microtubules |
| GO:0005875 microtubule associated complex | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP binds tubulin and colocalizes with microtubules. Reason: Cytoskeletal association is linked to its role in GABA(A) receptor trafficking and is not part of its core autophagy function. Actin cytoskeleton association is weakly supported. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Colocalizes with microtubules |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP co-localizes with GABA(A) receptor clusters in cultured neurons. Reason: GABARAP is mainly on intracellular membranes (Golgi, postsynaptic cisternae) and acts in receptor trafficking rather than residing in the plasma membrane; the location is peripheral. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Largely associated with intracellular membrane structures including the Golgi apparatus and postsynaptic cisternae |
| GO:0005886 plasma membrane | TAS PMID:9892355 GABA(A)-receptor-associated protein links GABA(A) receptors ... | KEEP AS NON CORE | Summary: GABARAP co-localizes with GABA(A) receptor clusters in cultured neurons. Reason: GABARAP is mainly on intracellular membranes (Golgi, postsynaptic cisternae) and acts in receptor trafficking rather than residing in the plasma membrane; the location is peripheral. Supporting Evidence: PMID:9892355 GABARAP binds to GABA(A) receptors both in vitro and in vivo, and co-localizes with the punctate staining of GABA(A) receptors on cultured cortical neurons. |
| GO:0005930 axoneme | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP has been reported in puncta along the ciliary axoneme. Reason: Transferred from mouse; not a core location. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Also localizes to discrete punctae along the ciliary axoneme |
| GO:0005930 axoneme | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: GABARAP has been reported in puncta along the ciliary axoneme. Reason: Transferred from mouse; not a core location. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Also localizes to discrete punctae along the ciliary axoneme |
| GO:0006605 protein targeting | TAS PMID:9892355 GABA(A)-receptor-associated protein links GABA(A) receptors ... | KEEP AS NON CORE | Summary: GABARAP has been proposed to link GABA(A) receptors to the cytoskeleton for their targeting and clustering. Reason: A genuine secondary role in neuronal receptor trafficking; the generic protein targeting term is acceptable but non-core. Supporting Evidence: PMID:9892355 The interactions among GABA(A) receptors, GABARAP and tubulin suggest a mechanism for the targeting and clustering of GABA(A) receptors. |
| GO:0006995 cellular response to nitrogen starvation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Atg8-family proteins act in starvation-induced autophagy. Reason: Nitrogen starvation is the yeast paradigm; GABARAP contributes to starvation autophagy in human cells, but the response term is context rather than function. Supporting Evidence: PMID:27864321 identify GABARAP subfamily members as primary contributors to PINK1/Parkin mitophagy and starvation autophagy |
| GO:0007268 chemical synaptic transmission | TAS PMID:9892355 GABA(A)-receptor-associated protein links GABA(A) receptors ... | MARK AS OVER ANNOTATED | Summary: GABARAP binds GABA(A) receptor gamma2 subunits and may affect their trafficking. Reason: Any effect on synaptic transmission is indirect, via receptor trafficking; chemical synaptic transmission is too broad and overstates the role. Supporting Evidence: PMID:9892355 The interactions among GABA(A) receptors, GABARAP and tubulin suggest a mechanism for the targeting and clustering of GABA(A) receptors. |
| GO:0008017 microtubule binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP binds tubulin/microtubules through its basic N-terminus. Reason: Supported by binding studies; secondary to its Atg8-family function. Supporting Evidence: PMID:9892355 the N terminus of GABARAP is highly positively charged and features a putative tubulin-binding motif |
| GO:0008429 phosphatidylethanolamine binding | IBA GO_REF:0000033 | ACCEPT | Summary: GABARAP is converted to a membrane-associated form II by phosphatidylethanolamine conjugation. Reason: Core Atg8-family property; GO represents Atg8 lipidation with this binding term. Supporting Evidence: PMID:15169837 two other mammalian homologues of yeast Atg8, gamma-aminobutyric-acid-type-A-receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE16) also generate form II, which are recovered in membrane fractions PMID:15169837 These results suggest that all mammalian Atg8 homologues receive a common modification to associate with autophagosomal membrane as the form II. |
| GO:0008429 phosphatidylethanolamine binding | IDA PMID:15169837 LC3, GABARAP and GATE16 localize to autophagosomal membrane ... | ACCEPT | Summary: GABARAP is converted to a membrane-associated form II by phosphatidylethanolamine conjugation. Reason: Core Atg8-family property; GO represents Atg8 lipidation with this binding term. Supporting Evidence: PMID:15169837 two other mammalian homologues of yeast Atg8, gamma-aminobutyric-acid-type-A-receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE16) also generate form II, which are recovered in membrane fractions PMID:15169837 These results suggest that all mammalian Atg8 homologues receive a common modification to associate with autophagosomal membrane as the form II. |
| GO:0008625 extrinsic apoptotic signaling pathway via death domain receptors | IDA PMID:15977068 GABAA receptor-associated protein (GABARAP) induces apoptosi... | MARK AS OVER ANNOTATED | Summary: Co-overexpression of GABARAP and DDX47 induced apoptosis in a tumor cell line. Reason: An overexpression phenotype; the cached abstract does not connect GABARAP to death-domain receptor signalling, and no physiological role in the extrinsic pathway is established. Supporting Evidence: PMID:15977068 co-transfection of GABARAP and DDX47 cDNA into a tumor cell line induces apoptosis |
| GO:0012505 endomembrane system | IEA GO_REF:0000044 | ACCEPT | Summary: GABARAP-II is a lipid-anchored peripheral protein of intracellular membranes, mainly autophagosomes. Reason: Correct general location. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. |
| GO:0012505 endomembrane system | ISS GO_REF:0000024 | ACCEPT | Summary: GABARAP-II is a lipid-anchored peripheral protein of intracellular membranes, mainly autophagosomes. Reason: Correct general location. Supporting Evidence: PMID:15169837 two other mammalian homologues of yeast Atg8, gamma-aminobutyric-acid-type-A-receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE16) also generate form II, which are recovered in membrane fractions |
| GO:0015629 actin cytoskeleton | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP binds tubulin and colocalizes with microtubules. Reason: Cytoskeletal association is linked to its role in GABA(A) receptor trafficking and is not part of its core autophagy function. Actin cytoskeleton association is weakly supported. Supporting Evidence: file:human/GABARAP/GABARAP-uniprot.txt Colocalizes with microtubules |
| GO:0016236 macroautophagy | IEA GO_REF:0000117 | ACCEPT | Summary: GABARAP functions in macroautophagy. Reason: Core process. Supporting Evidence: PMID:27864321 identify GABARAP subfamily members as primary contributors to PINK1/Parkin mitophagy and starvation autophagy |
| GO:0031410 cytoplasmic vesicle | IEA GO_REF:0000044 | ACCEPT | Summary: GABARAP-II is a lipid-anchored peripheral protein of intracellular membranes, mainly autophagosomes. Reason: Correct general location. Supporting Evidence: PMID:15169837 Generation of the form II correlates with autophagosome association of GABARAP and GATE16. |
| GO:0031410 cytoplasmic vesicle | ISS GO_REF:0000024 | ACCEPT | Summary: GABARAP-II is a lipid-anchored peripheral protein of intracellular membranes, mainly autophagosomes. Reason: Correct general location. Supporting Evidence: PMID:15169837 two other mammalian homologues of yeast Atg8, gamma-aminobutyric-acid-type-A-receptor-associated protein (GABARAP) and Golgi-associated ATPase enhancer of 16 kDa (GATE16) also generate form II, which are recovered in membrane fractions |
| GO:0031625 ubiquitin protein ligase binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. Supporting Evidence: PMID:25127057 TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. Supporting Evidence: PMID:25127057 TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. Supporting Evidence: PMID:25127057 TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. Supporting Evidence: PMID:25127057 TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. Supporting Evidence: PMID:25127057 TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:25127057 TRIM proteins regulate autophagy and can target autophagic s... | KEEP AS NON CORE | Summary: GABARAP binds LIR-containing E3 ubiquitin ligases, including TRIM proteins and CUL3 substrate adaptors. Reason: Real interactions that recruit ligases to GABARAP-positive membranes, but they are instances of general LIR docking rather than a distinct GABARAP function. Supporting Evidence: PMID:25127057 TRIMs associate with autophagy factors and act as platforms assembling ULK1 and Beclin 1 in their activated states |
| GO:0032436 positive regulation of proteasomal ubiquitin-dependent protein catabolic process | IMP PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | KEEP AS NON CORE | Summary: GABARAP proteins bind the CUL3 adaptors KBTBD6/KBTBD7 and are required for CUL3-KBTBD6/7 ubiquitylation and degradation of TIAM1. Reason: GABARAP acts as a membrane scaffold that localizes the ligase; supported by loss-of-function data, but a secondary function. Supporting Evidence: PMID:25684205 Surprisingly, ubiquitylation and degradation of TIAM1 by CUL3(KBTBD6/KBTBD7) depends on its binding to GABARAP proteins. PMID:25684205 we uncovered a previously unknown function of GABARAP proteins as membrane-localized signaling scaffolds |
| GO:0035020 regulation of Rac protein signal transduction | IMP PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | KEEP AS NON CORE | Summary: By supporting CUL3-KBTBD6/7-mediated TIAM1 degradation, GABARAP proteins restrict RAC1 signalling spatially. Reason: Indirect regulatory role through a ligase scaffold; non-core. Supporting Evidence: PMID:25684205 Surprisingly, ubiquitylation and degradation of TIAM1 by CUL3(KBTBD6/KBTBD7) depends on its binding to GABARAP proteins. PMID:25684205 we uncovered a previously unknown function of GABARAP proteins as membrane-localized signaling scaffolds |
| GO:0048487 beta-tubulin binding | IDA PMID:9892355 GABA(A)-receptor-associated protein links GABA(A) receptors ... | KEEP AS NON CORE | Summary: GABARAP interacts with tubulin. Reason: Experimental tubulin binding linked to its proposed role in GABA(A) receptor clustering; a secondary activity. Supporting Evidence: PMID:9892355 The interactions among GABA(A) receptors, GABARAP and tubulin suggest a mechanism for the targeting and clustering of GABA(A) receptors. PMID:9892355 the N terminus of GABARAP is highly positively charged and features a putative tubulin-binding motif |
| GO:0050811 GABA receptor binding | IBA GO_REF:0000033 | ACCEPT | Summary: GABARAP binds the intracellular loop of the GABA(A) receptor gamma2 subunit. Reason: Founding function of GABARAP, shown in vitro and in vivo and conserved in the GABARAP subclade; distinct from its autophagy role. Supporting Evidence: PMID:9892355 GABARAP binds to GABA(A) receptors both in vitro and in vivo, and co-localizes with the punctate staining of GABA(A) receptors on cultured cortical neurons. |
| GO:0050811 GABA receptor binding | IPI PMID:9892355 GABA(A)-receptor-associated protein links GABA(A) receptors ... | ACCEPT | Summary: GABARAP binds the intracellular loop of the GABA(A) receptor gamma2 subunit. Reason: Founding function of GABARAP, shown in vitro and in vivo and conserved in the GABARAP subclade; distinct from its autophagy role. Supporting Evidence: PMID:9892355 GABARAP binds to GABA(A) receptors both in vitro and in vivo, and co-localizes with the punctate staining of GABA(A) receptors on cultured cortical neurons. |
| GO:0061709 reticulophagy | IDA PMID:39284914 ER-phagy restrains inflammatory responses through its recept... | ACCEPT | Summary: GABARAP on autophagosomes binds the LIR of the ER-phagy receptor UBAC2 to promote selective ER degradation. Reason: Direct evidence that GABARAP engages an ER-phagy receptor; selective autophagy by LIR-receptor docking is a core Atg8 role. Supporting Evidence: PMID:39284914 UBAC2 harbors a canonical LC3-interacting region (LIR) in its cytoplasmic domain, which binds to autophagosomal GABARAP. |
| GO:0097225 sperm midpiece | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Transferred from mouse data placing GABARAP in the sperm midpiece. Reason: Tissue-specific location without evidence of a distinct function in human sperm. |
| GO:0097352 autophagosome maturation | IBA GO_REF:0000033 | ACCEPT | Summary: GABARAP-subfamily proteins recruit PLEKHM1 and govern autophagosome-lysosome fusion. Reason: Core function: GABARAPs are the main Atg8 subfamily for the maturation/fusion step. Supporting Evidence: PMID:27864321 We find that the GABARAP subfamily promotes PLEKHM1 recruitment and governs autophagosome-lysosome fusion, whereas the LC3 subfamily plays a less prominent role in these processes. PMID:20418806 our results indicate that LC3s are involved in elongation of the phagophore membrane whereas the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation |
| GO:0098696 regulation of neurotransmitter receptor localization to postsynaptic specialization membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP participates in trafficking of GABA(A) receptors in neurons. Reason: Transferred from mouse; consistent with the GABA receptor binding function but secondary to autophagy. Supporting Evidence: PMID:9892355 The interactions among GABA(A) receptors, GABARAP and tubulin suggest a mechanism for the targeting and clustering of GABA(A) receptors. |
| GO:0098982 GABA-ergic synapse | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GABARAP participates in trafficking of GABA(A) receptors in neurons. Reason: Transferred from mouse; consistent with the GABA receptor binding function but secondary to autophagy. Supporting Evidence: PMID:9892355 The interactions among GABA(A) receptors, GABARAP and tubulin suggest a mechanism for the targeting and clustering of GABA(A) receptors. |
| GO:0140311 protein sequestering activity | IDA PMID:34597140 GABARAP sequesters the FLCN-FNIP tumor suppressor complex to... | ACCEPT | Summary: Membrane-conjugated GABARAP binds a LIR in FNIP1/2 and sequesters the FLCN-FNIP complex on GABARAP-positive membranes, blocking its GAP activity toward RagC/D. Reason: Direct binding and sequestration evidence; this activity explains the TFEB/TFE3 and lysosome biogenesis phenotypes and is specific to GABARAP over LC3. Supporting Evidence: PMID:34597140 GABARAP directly binds to a previously unidentified LC3-interacting motif (LIR) in the FLCN/FNIP tumor suppressor complex and mediates sequestration to GABARAP-conjugated membrane compartments. PMID:34597140 This disrupts FLCN/FNIP GAP function toward RagC/D, resulting in impaired substrate-specific mTOR-dependent phosphorylation of TFEB. |
| GO:0140311 protein sequestering activity | IDA PMID:39423796 A TBK1-independent primordial function of STING in lysosomal... | ACCEPT | Summary: Membrane-conjugated GABARAP binds a LIR in FNIP1/2 and sequesters the FLCN-FNIP complex on GABARAP-positive membranes, blocking its GAP activity toward RagC/D. Reason: Direct binding and sequestration evidence; this activity explains the TFEB/TFE3 and lysosome biogenesis phenotypes and is specific to GABARAP over LC3. Supporting Evidence: PMID:39423796 GABARAP lipidation is known to inhibit the FLCN-FNIP-RagC/D axis, thus blocking mTORC1-mediated TFEB phosphorylation PMID:39423796 GABARAP lipidation, stimulated by the channel of STING, is key for STING-dependent TFEB activation. |
| GO:1902524 positive regulation of protein K48-linked ubiquitination | IMP PMID:25684205 CUL3-KBTBD6/KBTBD7 ubiquitin ligase cooperates with GABARAP ... | KEEP AS NON CORE | Summary: GABARAP proteins bind the CUL3 adaptors KBTBD6/KBTBD7 and are required for CUL3-KBTBD6/7 ubiquitylation and degradation of TIAM1. Reason: GABARAP acts as a membrane scaffold that localizes the ligase; supported by loss-of-function data, but a secondary function. Supporting Evidence: PMID:25684205 Surprisingly, ubiquitylation and degradation of TIAM1 by CUL3(KBTBD6/KBTBD7) depends on its binding to GABARAP proteins. PMID:25684205 we uncovered a previously unknown function of GABARAP proteins as membrane-localized signaling scaffolds |
| GO:1904262 negative regulation of TORC1 signaling | IDA PMID:34597140 GABARAP sequesters the FLCN-FNIP tumor suppressor complex to... | KEEP AS NON CORE | Summary: GABARAP sequestration of FLCN-FNIP impairs substrate-specific mTORC1 phosphorylation of TFEB. Reason: Effect is restricted to the non-canonical, RagC/D-dependent TFEB branch rather than TORC1 signalling broadly; acceptable as a downstream consequence. Supporting Evidence: PMID:34597140 This disrupts FLCN/FNIP GAP function toward RagC/D, resulting in impaired substrate-specific mTOR-dependent phosphorylation of TFEB. |
| GO:1904262 negative regulation of TORC1 signaling | IDA PMID:39423796 A TBK1-independent primordial function of STING in lysosomal... | KEEP AS NON CORE | Summary: GABARAP sequestration of FLCN-FNIP impairs substrate-specific mTORC1 phosphorylation of TFEB. Reason: Effect is restricted to the non-canonical, RagC/D-dependent TFEB branch rather than TORC1 signalling broadly; acceptable as a downstream consequence. Supporting Evidence: PMID:39423796 GABARAP lipidation is known to inhibit the FLCN-FNIP-RagC/D axis, thus blocking mTORC1-mediated TFEB phosphorylation |
| GO:1905673 positive regulation of lysosome organization | IDA PMID:34597140 GABARAP sequesters the FLCN-FNIP tumor suppressor complex to... | ACCEPT | Summary: GABARAP lipidation is needed for TFEB/TFE3 activation and lysosomal biogenesis in response to CASM, mitophagy, xenophagy and STING activation. Reason: Direct consequence of FLCN-FNIP sequestration by membrane-conjugated GABARAP; a GABARAP-specific function not shared with LC3. Supporting Evidence: PMID:34597140 the membrane conjugation of GABARAP, but not LC3, is required for activation of TFEB/TFE3 to control lysosomal capacity |
| GO:1905673 positive regulation of lysosome organization | IDA PMID:39423796 A TBK1-independent primordial function of STING in lysosomal... | ACCEPT | Summary: GABARAP lipidation is needed for TFEB/TFE3 activation and lysosomal biogenesis in response to CASM, mitophagy, xenophagy and STING activation. Reason: Direct consequence of FLCN-FNIP sequestration by membrane-conjugated GABARAP; a GABARAP-specific function not shared with LC3. Supporting Evidence: PMID:39423796 GABARAP lipidation, stimulated by the channel of STING, is key for STING-dependent TFEB activation. |
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Download this section (compressed HTML)Q: Is the GABA(A) receptor trafficking role of GABARAP lipidation-dependent, and does it use the same LIR-docking site as autophagy partners?
Q: Which GABARAP functions (PLEKHM1 recruitment, FLCN-FNIP sequestration) are shared with GABARAPL1 and GABARAPL2, and which are specific to GABARAP?
Experiment: Re-express GABARAP alone, or LIR-docking-site mutants, in Atg8 hexa-knockout cells and measure PLEKHM1 recruitment, autophagosome-lysosome fusion and TFEB nuclear translocation.
Hypothesis: GABARAP alone is sufficient to restore fusion and FLCN-FNIP-dependent TFEB activation.
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