ATG9A is a phospholipid scramblase protein that mediates autophagosomal membrane expansion (PMID: 22456507, 27510922, 32513819, 32610138). It is the only transmembrane protein of the core autophagy machinery. ATG9A has six transmembrane helices which self-oligomerize to form a homotrimer (PMID: 32610138). ATG9A is composed of two distinct domains, a transmembrane domain (TMD; 1–525) and a C-terminal IDR (526–839). The TMD of ATG9A forms an interlocked trimer and functions as a lipid scramblase (PMID: 33106659, 32610138, 33106658). ATG9A distributes lipids coming from endoplasmic reticulum (ER), transported via ATG2 proteins, across the growing phagophore from the outer to the inner leaflet (PMID: 33106658, 31883797). ATG9A forms Golgi-derived vesicles, which are recruited to autophagy initiation sites through a complex trafficking process (PMID: 34257406, 30262884, 29180427, 26711178). ATG9 knockout mice resulted in impaired autophagosome biogenesis and accumulation of p62 (PMID: 19926846).
Monomer
Representations
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