| Primary Identifier | IPR007241 | Type | Family |
| Short Name | Autophagy-rel_prot_9 |
| description | Macroautophagy is a bulk degradation process induced by starvation in eukaryotic cells. In yeast, 15 Atg proteins coordinate the formation of autophagosomes. The pre-autophagosomal structure contains at least five Atg proteins: Atg1p, Atg2p, Atg5p, Aut7p/Atg8p and Atg16p, found in the vacuole [, ]. The C-terminal glycine of Atg12p is conjugated to a lysine residue of Atg5p via an isopeptide bond. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. Autophagy protein 16 (Atg16) has been shown to bind to Atg5 and is required for the function of the Atg12p-Atg5p conjugate []. Autophagy protein 5 (Atg5) is directly required for the import of aminopeptidase I via the cytoplasm-to-vacuole targeting pathway [].Atg9 plays a direct role in the formation of the cytoplasm to vacuole targeting and autophagic vesicles. It colocalizes with Atg2 at the expanding edge of the isolation membrane and acts as a lipid scramblase that translocates phospholipids delivered by Atg2 from the cytoplasmic to the luminal leaflet [, ]. |
