BAIT
ATG8
APG8, AUT7, CVT5, ubiquitin-like protein ATG8, L000004607, L000004604, YBL078C
Component of autophagosomes and Cvt vesicles; regulator of Atg1p, targets it to autophagosomes; binds the Atg1p-Atg13p complex, triggering its vacuolar degradation; unique ubiquitin-like protein whose conjugation target is lipid phosphatidylethanolamine (PE); Atg8p-PE is anchored to membranes, is involved in phagophore expansion, and may mediate membrane fusion during autophagosome formation; deconjugation of Atg8p-PE is required for efficient autophagosome biogenesis
GO Process (9)
GO Function (1)
GO Component (5)
Gene Ontology Biological Process
- CVT pathway [IMP]
- ER to Golgi vesicle-mediated transport [IGI, IMP, IPI]
- autophagic vacuole assembly [IMP]
- cellular protein complex localization [IMP]
- late nucleophagy [IMP]
- membrane fusion [IDA, IMP]
- mitochondrion degradation [IMP]
- piecemeal microautophagy of nucleus [IMP]
- protein targeting to vacuole involved in autophagy [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
ATG4B
APG4B, AUTL1
autophagy related 4B, cysteine peptidase
GO Process (11)
GO Function (4)
GO Component (2)
Gene Ontology Biological Process
- C-terminal protein lipidation [IBA]
- autophagic vacuole assembly [IGI]
- autophagy [IGI]
- cellular response to nitrogen starvation [IBA]
- mitochondrion degradation [IBA]
- nucleophagy [IBA]
- positive regulation of autophagy [IDA]
- protein delipidation [IBA]
- protein processing [IBA]
- protein targeting to membrane [IBA]
- proteolysis [IDA]
Gene Ontology Molecular Function
Homo sapiens
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
Nix is a selective autophagy receptor for mitochondrial clearance.
Autophagy is the cellular homeostatic pathway that delivers large cytosolic materials for degradation in the lysosome. Recent evidence indicates that autophagy mediates selective removal of protein aggregates, organelles and microbes in cells. Yet, the specificity in targeting a particular substrate to the autophagy pathway remains poorly understood. Here, we show that the mitochondrial protein Nix is a selective autophagy receptor ... [more]
EMBO Rep. Jan. 01, 2010; 11(1);45-51 [Pubmed: 20010802]
Throughput
- Low Throughput
Curated By
- BioGRID