ATG2A
Domain
The chorein N-terminal domain mediates lipid transfer activity.
Function
Lipid transfer protein involved in autophagosome assembly (PubMed:28561066, PubMed:30952800, PubMed:31271352). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (PubMed:30952800, PubMed:31271352). Binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, and extracts phospholipids from the membrane source and transfers them to ATG9 (ATG9A or ATG9B) to the IM for membrane expansion (PubMed:30952800, PubMed:31271352). Lipid transfer activity is enhanced by WIPI1 and WDR45/WIPI4, which promote ATG2A-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes (PubMed:31271352). Also regulates lipid droplets morphology and distribution within the cell (PubMed:22219374, PubMed:28561066).
Sequence Similarities
Belongs to the ATG2 family.
Cellular localization
- Preautophagosomal structure membrane
- Peripheral membrane protein
- Lipid droplet
- Endoplasmic reticulum membrane
- Peripheral membrane protein
- Localizes to endoplasmic reticulum-autophagosome contact sites.
Alternative names
KIAA0404, ATG2A, Autophagy-related protein 2 homolog A