Atg8 is a ubiquitin-like autophagy protein that is proteolytically processed at its C terminus and conjugated to phosphatidylethanolamine on phagophore, autophagosome, and Cvt vesicle membranes. Membrane-bound Atg8 tethers and hemifuses membranes during phagophore expansion and autophagosome maturation, and it presents an Atg8-family docking surface for selective-autophagy receptors and other Atg proteins. In Saccharomyces cerevisiae it supports starvation-induced macroautophagy and selective routes including the Cvt pathway, mitophagy, ER-phagy, nucleophagy, and vacuolar membrane remodeling.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000045 autophagosome assembly | IBA GO_REF:0000033 | ACCEPT | Summary: Accept autophagosome assembly as a conserved, core Atg8 function. Reason: Atg8-PE is required for phagophore expansion into autophagosomes; direct yeast experiments and the eukaryotic ATG8-family PAINT node PTN000103522 both support this core function. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000103522 · eukaryotic ATG8-family node SUPPORTS TRANSFER The PTHR10969 PAINT IBD node places this assertion on a clade that includes S. cerevisiae Atg8. |
| GO:0000045 autophagosome assembly | IMP PMID:11149920 Membrane recruitment of Aut7p in the autophagy and cytoplasm... | ACCEPT | Summary: Accept autophagosome assembly as a conserved, core Atg8 function. Reason: Atg8-PE is required for phagophore expansion into autophagosomes; direct yeast experiments and the eukaryotic ATG8-family PAINT node PTN000103522 both support this core function. Supporting Evidence: |
| GO:0000329 fungal-type vacuole membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Keep fungal vacuole-membrane localization as valid but secondary. Reason: Atg8 can act at the fungal vacuole membrane, including Hfl1-dependent early-stationary-phase turnover of vacuolar membrane proteins; PTN000861115 captures a fungal Atg8 clade with this localization, but it is secondary to the phagophore/autophagosome role. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000861115 · fungal Atg8 vacuole-membrane node SUPPORTS TRANSFER The fungal PTN000861115 IBD node is supported by SGD:S000000174 and PomBase:SPBP8B7.24c and safely transfers a fungal-type vacuole membrane localization to S. cerevisiae Atg8. |
| GO:0000329 fungal-type vacuole membrane | IDA PMID:10837468 Aut7p, a soluble autophagic factor, participates in multiple... | KEEP AS NON CORE | Summary: Keep fungal vacuole-membrane localization as valid but secondary. Reason: Atg8 can act at the fungal vacuole membrane, including Hfl1-dependent early-stationary-phase turnover of vacuolar membrane proteins; PTN000861115 captures a fungal Atg8 clade with this localization, but it is secondary to the phagophore/autophagosome role. |
| GO:0000329 fungal-type vacuole membrane | IPI PMID:10837468 Aut7p, a soluble autophagic factor, participates in multiple... | KEEP AS NON CORE | Summary: Keep fungal vacuole-membrane localization as valid but secondary. Reason: Atg8 can act at the fungal vacuole membrane, including Hfl1-dependent early-stationary-phase turnover of vacuolar membrane proteins; PTN000861115 captures a fungal Atg8 clade with this localization, but it is secondary to the phagophore/autophagosome role. |
| GO:0000407 phagophore assembly site | IDA PMID:11689437 The pre-autophagosomal structure organized by concerted func... | ACCEPT | Summary: Accept phagophore assembly site localization. Reason: Multiple GFP-Atg8 imaging studies place Atg8 at the perivacuolar phagophore assembly site where Cvt vesicles and autophagosomes form. Supporting Evidence: |
| GO:0000407 phagophore assembly site | IDA PMID:15659643 Atg11 links cargo to the vesicle-forming machinery in the cy... | ACCEPT | Summary: Accept phagophore assembly site localization. Reason: Multiple GFP-Atg8 imaging studies place Atg8 at the perivacuolar phagophore assembly site where Cvt vesicles and autophagosomes form. Supporting Evidence: |
| GO:0000407 phagophore assembly site | IDA PMID:16680092 Two newly identified sites in the ubiquitin-like protein Atg... | ACCEPT | Summary: Accept phagophore assembly site localization. Reason: Multiple GFP-Atg8 imaging studies place Atg8 at the perivacuolar phagophore assembly site where Cvt vesicles and autophagosomes form. Supporting Evidence: |
| GO:0000407 phagophore assembly site | IDA PMID:19398890 Mutation at the cargo-receptor binding site of Atg8 also aff... | ACCEPT | Summary: Accept phagophore assembly site localization. Reason: Multiple GFP-Atg8 imaging studies place Atg8 at the perivacuolar phagophore assembly site where Cvt vesicles and autophagosomes form. Supporting Evidence: |
| GO:0000407 phagophore assembly site | IDA PMID:23129774 Atg9 vesicles recruit vesicle-tethering proteins Trs85 and Y... | ACCEPT | Summary: Accept phagophore assembly site localization. Reason: Multiple GFP-Atg8 imaging studies place Atg8 at the perivacuolar phagophore assembly site where Cvt vesicles and autophagosomes form. Supporting Evidence: |
| GO:0000421 autophagosome membrane | IBA GO_REF:0000033 | ACCEPT | Summary: Accept autophagosome membrane localization as a core Atg8-family placement. Reason: Atg8 is lipidated on expanding phagophore/autophagosome membranes, and the PTN000103522 PAINT node places this conserved autophagosome-membrane role at the eukaryotic ATG8 family node. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000103522 · eukaryotic ATG8-family node SUPPORTS TRANSFER The PTHR10969 PAINT IBD node places this assertion on a clade that includes S. cerevisiae Atg8. |
| GO:0000421 autophagosome membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Accept autophagosome membrane localization as a core Atg8-family placement. Reason: Atg8 is lipidated on expanding phagophore/autophagosome membranes, and the PTN000103522 PAINT node places this conserved autophagosome-membrane role at the eukaryotic ATG8 family node. |
| GO:0000422 autophagy of mitochondrion | IMP PMID:19793921 A genomic screen for yeast mutants defective in selective mi... | ACCEPT | Summary: Accept mitophagy/autophagy of mitochondria. Reason: A yeast mutant screen found ATG8 among the autophagy genes required for selective mitochondrial autophagy. Supporting Evidence: |
| GO:0000423 mitophagy | IBA GO_REF:0000033 | ACCEPT | Summary: Accept mitophagy as an inherited selective-autophagy function. Reason: Mitophagy uses the conserved ATG8-family machinery; the PTN000103522 PAINT placement is compatible with the direct yeast mitophagy requirement for ATG8. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000103522 · eukaryotic ATG8-family node SUPPORTS TRANSFER The PTHR10969 PAINT IBD node places this assertion on a clade that includes S. cerevisiae Atg8. |
| GO:0005515 protein binding | IPI PMID:10688190 A comprehensive analysis of protein-protein interactions in ... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:10837468 Aut7p, a soluble autophagic factor, participates in multiple... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:11100732 A ubiquitin-like system mediates protein lipidation. | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:11100732 A ubiquitin-like system mediates protein lipidation. | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:11283351 A comprehensive two-hybrid analysis to explore the yeast pro... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:12965207 The carboxyl terminal 17 amino acids within Apg7 are essenti... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:18719252 High-quality binary protein interaction map of the yeast int... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:19250911 A role for NBR1 in autophagosomal degradation of ubiquitinat... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: PMID:19250911 studies human NBR1/p62 selective-autophagy receptor biology, and this IntAct row reflects a heterologous S. cerevisiae Atg8 assay rather than an endogenous yeast ATG8 function. In any case, GO:0005515 is an uninformative molecular-function term for Atg8-family receptor docking. Supporting Evidence: PMID:19250911 is an autophagy receptor containing LC3- and ubiquitin |
| GO:0005515 protein binding | IPI PMID:19250911 A role for NBR1 in autophagosomal degradation of ubiquitinat... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: PMID:19250911 studies human NBR1/p62 selective-autophagy receptor biology, and this IntAct row reflects a heterologous S. cerevisiae Atg8 assay rather than an endogenous yeast ATG8 function. In any case, GO:0005515 is an uninformative molecular-function term for Atg8-family receptor docking. Supporting Evidence: PMID:19250911 is an autophagy receptor containing LC3- and ubiquitin |
| GO:0005515 protein binding | IPI PMID:19285500 The amino-terminal region of Atg3 is essential for associati... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:20010802 Nix is a selective autophagy receptor for mitochondrial clea... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: Novak et al. used S. cerevisiae Atg8 as bait in a heterologous yeast two-hybrid screen to identify and characterize the mammalian mitophagy receptor Nix/BNIP3L. The assay does not establish an endogenous yeast ATG8 function, and in any case GO:0005515 is uninformative. Supporting Evidence: PMID:20010802 To search for proteins that interact with autophagy-specific UBL proteins, we used Saccharomyces cerevisiae (Sc)Atg8 as bait in yeast two-hybrid screens. |
| GO:0005515 protein binding | IPI PMID:20200478 Nix, a receptor protein for mitophagy in mammals. | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: PMID:20200478 studies the mammalian Nix/LC3-GABARAP mitophagy receptor interaction, with the GOA supporting entity pointing to human BNIP3L rather than a physiological yeast Atg8 partner. This does not establish an endogenous yeast ATG8 molecular function, and GO:0005515 is uninformative for Atg8-family receptor docking. Supporting Evidence: PMID:20200478 Nix is a mitochondrial receptor that can directly connect to one of the autophagic machinery components, the Atg8 homologs LC3 and GABARAP |
| GO:0005515 protein binding | IPI PMID:21617041 Phosphorylation of the autophagy receptor optineurin restric... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: Wild et al. study the human OPTN LC3/GABARAP receptor interaction in mammalian antibacterial autophagy, with the GOA supporting entity pointing to human OPTN rather than a physiological yeast Atg8 partner. This row does not establish an endogenous yeast ATG8 molecular function, and GO:0005515 is uninformative for Atg8-family receptor docking. Supporting Evidence: PMID:21617041 OPTN bound to ubiquitin chains and autophagy modifiers ATG8/LC3/GABARAP proteins |
| GO:0005515 protein binding | IPI PMID:22056771 Insights into noncanonical E1 enzyme activation from the str... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:22056771 Insights into noncanonical E1 enzyme activation from the str... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:22885598 Binding of the Atg1/ULK1 kinase to the ubiquitin-like protei... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:23142976 Noncanonical E2 recruitment by the autophagy E1 revealed by ... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:23142976 Noncanonical E2 recruitment by the autophagy E1 revealed by ... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:24705553 Cargo binding to Atg19 unmasks additional Atg8 binding sites... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:24705553 Cargo binding to Atg19 unmasks additional Atg8 binding sites... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:25042851 Autophagic clearance of polyQ proteins mediated by ubiquitin... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:25042851 Autophagic clearance of polyQ proteins mediated by ubiquitin... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:25042851 Autophagic clearance of polyQ proteins mediated by ubiquitin... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:26040717 Receptor-mediated selective autophagy degrades the endoplasm... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:26040717 Receptor-mediated selective autophagy degrades the endoplasm... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:37968396 The social and structural architecture of the yeast protein ... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005515 protein binding | IPI PMID:9649430 Aut2p and Aut7p, two novel microtubule-associated proteins a... | REMOVE | Summary: Remove uninformative protein-binding annotation. Reason: The cited IPI experiments identify Atg8 partners in conjugation, cargo-receptor docking, or selective-autophagy pathways, but the bare GO:0005515 term does not state an informative molecular function and should not be retained for these interactions. |
| GO:0005737 cytoplasm | IDA PMID:9649430 Aut2p and Aut7p, two novel microtubule-associated proteins a... | TOO GENERAL | Summary: Mark cytoplasm as too general relative to more specific Atg8 locations. Reason: Atg8 is present in the cytoplasm, but cytosol, phagophore assembly site, autophagosome, and membrane locations capture the experimentally supported compartments more precisely. Supporting Evidence: |
| GO:0005774 vacuolar membrane | EXP PMID:23549786 Fine mapping of autophagy-related proteins during autophagos... | MODIFY | Summary: Keep vacuolar membrane localization as contextual. Reason: Atg8 can accumulate or be recruited on the vacuolar membrane, but GO:0005774 is the generic parent of the accepted fungal-type vacuole membrane child GO:0000329. The fungal-specific term is the better replacement for S. cerevisiae Atg8. Proposed replacements: fungal-type vacuole membrane |
| GO:0005774 vacuolar membrane | EXP PMID:34088313 Membrane recruitment of Atg8 by Hfl1 facilitates turnover of... | MODIFY | Summary: Keep vacuolar membrane localization as contextual. Reason: He et al. support an early-stationary-phase vacuolar membrane role for Atg8, but GO:0005774 is the generic parent of the accepted fungal-type vacuole membrane child GO:0000329. The fungal-specific term is the better replacement for S. cerevisiae Atg8. Proposed replacements: fungal-type vacuole membrane Supporting Evidence: |
| GO:0005774 vacuolar membrane | IEA GO_REF:0000044 | MODIFY | Summary: Keep vacuolar membrane localization as contextual. Reason: The UniProt SubCell vacuolar-membrane mapping is compatible with Atg8 biology, but GO:0005774 is the generic parent of the accepted fungal-type vacuole membrane child GO:0000329. The fungal-specific term is the better replacement for S. cerevisiae Atg8. Proposed replacements: fungal-type vacuole membrane |
| GO:0005776 autophagosome | IDA PMID:10525546 Formation process of autophagosome is traced with Apg8/Aut7p... | ACCEPT | Summary: Accept autophagosome localization. Reason: Atg8 is recruited to forming autophagosomes and remains associated with completed autophagosomes before fusion with the vacuole. Supporting Evidence: |
| GO:0005776 autophagosome | IDA PMID:11149920 Membrane recruitment of Aut7p in the autophagy and cytoplasm... | ACCEPT | Summary: Accept autophagosome localization. Reason: Atg8 is recruited to forming autophagosomes and remains associated with completed autophagosomes before fusion with the vacuole. Supporting Evidence: |
| GO:0005776 autophagosome | IDA PMID:16079147 Trs85 (Gsg1), a component of the TRAPP complexes, is require... | ACCEPT | Summary: Accept autophagosome localization. Reason: Atg8 is recruited to forming autophagosomes and remains associated with completed autophagosomes before fusion with the vacuole. Supporting Evidence: |
| GO:0005811 lipid droplet | IDA PMID:28003432 Autophagy-independent function of Atg8 in lipid droplet dyna... | KEEP AS NON CORE | Summary: Keep lipid-droplet localization as a secondary stationary-phase role. Reason: Atg8 localizes to lipid droplets in stationary-phase cells and affects lipid-droplet number independently of canonical autophagic flux, a real but secondary role. Supporting Evidence: |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | KEEP AS NON CORE | Summary: Keep cytosol as a non-core Atg8 pool. Reason: Newly synthesized and delipidated Atg8 are soluble before membrane recruitment; this cytosolic pool is real but less descriptive than Atg8-PE function on autophagic membranes. Supporting Evidence: |
| GO:0005829 cytosol | IDA PMID:11149920 Membrane recruitment of Aut7p in the autophagy and cytoplasm... | KEEP AS NON CORE | Summary: Keep cytosol as a non-core Atg8 pool. Reason: Newly synthesized and delipidated Atg8 are soluble before membrane recruitment; this cytosolic pool is real but less descriptive than Atg8-PE function on autophagic membranes. Supporting Evidence: |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IGI PMID:10837468 Aut7p, a soluble autophagic factor, participates in multiple... | KEEP AS NON CORE | Summary: Keep ER-to-Golgi transport as a non-core early trafficking phenotype. Reason: Early yeast experiments reported AUT7/ATG8 genetic and physical interactions with ER-to-Golgi SNARE machinery; retain the direct experimental annotation as contextual rather than as Atg8's core autophagy function. Supporting Evidence: |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IMP PMID:10837468 Aut7p, a soluble autophagic factor, participates in multiple... | KEEP AS NON CORE | Summary: Keep ER-to-Golgi transport as a non-core early trafficking phenotype. Reason: Early yeast experiments reported AUT7/ATG8 genetic and physical interactions with ER-to-Golgi SNARE machinery; retain the direct experimental annotation as contextual rather than as Atg8's core autophagy function. Supporting Evidence: |
| GO:0006888 endoplasmic reticulum to Golgi vesicle-mediated transport | IPI PMID:10837468 Aut7p, a soluble autophagic factor, participates in multiple... | KEEP AS NON CORE | Summary: Keep ER-to-Golgi transport as a non-core early trafficking phenotype. Reason: Early yeast experiments reported AUT7/ATG8 genetic and physical interactions with ER-to-Golgi SNARE machinery; retain the direct experimental annotation as contextual rather than as Atg8's core autophagy function. Supporting Evidence: |
| GO:0006914 autophagy | IMP PMID:9649430 Aut2p and Aut7p, two novel microtubule-associated proteins a... | MODIFY | Summary: General autophagy should be refined to macroautophagy. Reason: The early ATG8 evidence concerns the macroautophagy/Cvt machinery that builds double-membrane Atg8-positive vesicles for vacuolar delivery; GO:0016236 macroautophagy is the more informative replacement for the generic GO:0006914 parent. Proposed replacements: macroautophagy Supporting Evidence: |
| GO:0006995 cellular response to nitrogen starvation | IBA GO_REF:0000033 | ACCEPT | Summary: Accept cellular response to nitrogen starvation for conserved Atg8 autophagy induction. Reason: Nitrogen starvation induces Atg8-dependent macroautophagy in yeast, and PTN000103522 places this stress-response function on the conserved eukaryotic ATG8-family node. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000103522 · eukaryotic ATG8-family node SUPPORTS TRANSFER The PTHR10969 PAINT IBD node places this assertion on a clade that includes S. cerevisiae Atg8. |
| GO:0008429 phosphatidylethanolamine binding | IBA GO_REF:0000033 | ACCEPT | Summary: Accept phosphatidylethanolamine binding. Reason: Atg8 is conjugated to phosphatidylethanolamine and the lipidated Atg8-PE form is the membrane-bound species that drives Atg8 function; PAINT assigns this molecular function to the eukaryotic ATG8 node PTN000103522. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000103522 · eukaryotic ATG8-family node SUPPORTS TRANSFER The PTHR10969 PAINT IBD node places this assertion on a clade that includes S. cerevisiae Atg8. |
| GO:0008429 phosphatidylethanolamine binding | IMP PMID:19398890 Mutation at the cargo-receptor binding site of Atg8 also aff... | ACCEPT | Summary: Accept phosphatidylethanolamine binding. Reason: Atg8 is conjugated to phosphatidylethanolamine and the lipidated Atg8-PE form is the membrane-bound species that drives Atg8 function; PAINT assigns this molecular function to the eukaryotic ATG8 node PTN000103522. Supporting Evidence: |
| GO:0016241 regulation of macroautophagy | IMP PMID:19398890 Mutation at the cargo-receptor binding site of Atg8 also aff... | MODIFY | Summary: Regulation of macroautophagy should be refined to macroautophagy. Reason: Mutations at the Atg8 cargo-receptor-binding site compromise the core Atg8 membrane and cargo-sorting functions that execute macroautophagy. The evidence shows participation in macroautophagy rather than upstream regulation of the pathway. Proposed replacements: macroautophagy Supporting Evidence: |
| GO:0031386 protein tag activity | IMP PMID:22652539 Dual roles of Atg8-PE deconjugation by Atg4 in autophagy. | ACCEPT | Summary: Accept protein tag activity for lipidated Atg8. Reason: Atg8 is a ubiquitin-like modifier whose reversible conjugation to PE creates an Atg8 tag on autophagic membranes for receptor and Atg-protein docking. Supporting Evidence: |
| GO:0031503 protein-containing complex localization | IMP PMID:22885598 Binding of the Atg1/ULK1 kinase to the ubiquitin-like protei... | ACCEPT | Summary: Accept protein-containing complex localization for Atg1 kinase complex targeting. Reason: Kraft et al. showed that direct Atg1-Atg8 binding targets the Atg1 kinase complex onto autophagic vesicles for vacuolar delivery. That is a protein-complex localization event; the separately accepted GO:0071211 row captures the pathway context but is not a child refinement of GO:0031503. Supporting Evidence: |
| GO:0031966 mitochondrial membrane | IDA PMID:30510114 The mitochondrial phosphatidylserine decarboxylase Psd1 is i... | KEEP AS NON CORE | Summary: Keep mitochondrial membrane localization as mitophagy-contextual. Reason: Atg8 is recruited to mitochondria during nitrogen-starvation mitophagy in respiratory carbon source, but this is a selective-autophagy location rather than Atg8's central phagophore/autophagosome site. Supporting Evidence: |
| GO:0031966 mitochondrial membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: Keep mitochondrial membrane localization as mitophagy-contextual. Reason: Atg8 is recruited to mitochondria during nitrogen-starvation mitophagy in respiratory carbon source, but this is a selective-autophagy location rather than Atg8's central phagophore/autophagosome site. |
| GO:0032258 cytoplasm to vacuole targeting by the Cvt pathway | IMP PMID:19398890 Mutation at the cargo-receptor binding site of Atg8 also aff... | ACCEPT | Summary: Accept the Cvt pathway as a core selective-autophagy pathway for Atg8. Reason: Atg8 is required for Cvt vesicle formation and for selective receptor-mediated prApe1 transport from cytoplasm to vacuole. Supporting Evidence: |
| GO:0032258 cytoplasm to vacuole targeting by the Cvt pathway | IMP PMID:9649430 Aut2p and Aut7p, two novel microtubule-associated proteins a... | ACCEPT | Summary: Accept the Cvt pathway as a core selective-autophagy pathway for Atg8. Reason: Atg8 is required for Cvt vesicle formation and for selective receptor-mediated prApe1 transport from cytoplasm to vacuole. Supporting Evidence: |
| GO:0033110 Cvt vesicle membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Accept Cvt vesicle membrane localization. Reason: Atg8 is recruited onto membranes that form Cvt vesicles in the constitutive cytoplasm-to-vacuole targeting pathway. |
| GO:0034497 protein localization to phagophore assembly site | IMP PMID:25680528 Localization of Atg3 to autophagy-related membranes and its ... | ACCEPT | Summary: Accept protein localization to the phagophore assembly site. Reason: Atg8-family interacting motif contacts with Atg3 enhance Atg3 localization to Atg8-positive autophagic membranes at the PAS and promote membrane expansion. Supporting Evidence: |
| GO:0034727 piecemeal microautophagy of the nucleus | IMP PMID:18701704 Piecemeal microautophagy of the nucleus requires the core ma... | ACCEPT | Summary: Accept piecemeal microautophagy of the nucleus. Reason: Piecemeal microautophagy of the nucleus is inhibited in atg8 mutant cells, supporting a direct requirement for ATG8 in this yeast nuclear microautophagy route. Supporting Evidence: |
| GO:0044804 nucleophagy | IMP PMID:22768199 A late form of nucleophagy in Saccharomyces cerevisiae. | ACCEPT | Summary: Accept nucleophagy. Reason: Late nucleophagy in Saccharomyces cerevisiae is blocked by loss of core autophagy genes including ATG8, supporting ATG8 involvement in this selective autophagy pathway. Supporting Evidence: |
| GO:0061025 membrane fusion | IDA PMID:17632063 Atg8, a ubiquitin-like protein required for autophagosome fo... | ACCEPT | Summary: Accept Atg8-mediated membrane fusion. Reason: Lipidated Atg8 directly mediates membrane tethering and hemifusion in vitro, and Atg8 mutants link that activity to autophagosomal membrane expansion in vivo. Supporting Evidence: |
| GO:0061025 membrane fusion | IMP PMID:17632063 Atg8, a ubiquitin-like protein required for autophagosome fo... | ACCEPT | Summary: Accept Atg8-mediated membrane fusion. Reason: Lipidated Atg8 directly mediates membrane tethering and hemifusion in vitro, and Atg8 mutants link that activity to autophagosomal membrane expansion in vivo. Supporting Evidence: |
| GO:0061709 reticulophagy | IMP PMID:26181331 A Role for Macro-ER-Phagy in ER Quality Control. | ACCEPT | Summary: Accept reticulophagy. Reason: Yeast ER-phagy requires the canonical Atg machinery; Atg8 supplies the autophagic membrane platform used by ER-phagy receptors such as Atg39 and Atg40. Supporting Evidence: |
| GO:0071211 protein targeting to vacuole involved in autophagy | IMP PMID:22885598 Binding of the Atg1/ULK1 kinase to the ubiquitin-like protei... | ACCEPT | Summary: Accept protein targeting to the vacuole during autophagy. Reason: Atg8 binds the Atg1 kinase through an AIM/LIR motif and helps deliver Atg1 to the vacuole in an autophagy-dependent manner. Supporting Evidence: |
| GO:0097352 autophagosome maturation | IBA GO_REF:0000033 | ACCEPT | Summary: Accept autophagosome maturation as a conserved Atg8-family process. Reason: Atg8-PE cycling promotes maturation of intermediate autophagosomal membranes into fusion-capable autophagosomes, and PTN000103522 places this function on the eukaryotic ATG8-family node. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000103522 · eukaryotic ATG8-family node SUPPORTS TRANSFER The PTHR10969 PAINT IBD node places this assertion on a clade that includes S. cerevisiae Atg8. |
| GO:0120095 vacuole-isolation membrane contact site | IDA PMID:23549786 Fine mapping of autophagy-related proteins during autophagos... | ACCEPT | Summary: Accept VICS localization during autophagosome formation. Reason: Fine mapping of autophagy proteins detected Atg8 at the vacuole-isolation membrane contact site and the cup-shaped isolation membrane during autophagosome formation. Supporting Evidence: |
| GO:0140042 lipid droplet formation | IMP PMID:28003432 Autophagy-independent function of Atg8 in lipid droplet dyna... | KEEP AS NON CORE | Summary: Keep lipid-droplet formation as a secondary function. Reason: Atg8 affects lipid-droplet accumulation in stationary phase through a lipidation-independent and autophagy-independent activity; retain the process as a secondary role. Supporting Evidence: |
| GO:1905153 regulation of membrane invagination | IMP PMID:31616012 Role of Atg8 in the regulation of vacuolar membrane invagina... | KEEP AS NON CORE | Summary: Keep regulation of vacuolar membrane invagination as secondary. Reason: Atg8 suppresses excessive heat-induced vacuolar membrane invagination independently of its canonical lipidation-dependent autophagy function. Supporting Evidence: |
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