2024年12月24日 · ATG2A (Autophagy Related 2A) is a Protein Coding gene. Diseases associated with ATG2A include Neurodegeneration With Brain Iron Accumulation and Neurodegeneration With Brain Iron Accumulation 5 . Among its related pathways are Alzheimer's disease and miRNA effects and Autophagy .

2024年8月2日 · ATG2A is a peripheral membrane protein that tethers membranes and transports lipids from donor membranes to the phagophore with the help of WIPI (WD-repeat protein interacting with...

2019年7月4日 · Autophagy-related 2 (ATG2), the rod-shaped protein that tethers phosphatidylinositol 3-phosphate (PI3P)-enriched phagophores to the endoplasmic reticulum (ER), is suggested to be essential for phagophore expansion, but the underlying mechanism remains unclear. Here, we demonstrate that human ATG2A is a lipid transfer protein.

2019年6月3日 · Here we show that the autophagy protein, ATG2, without a clear function since its discovery over 20 yr ago, is in fact a lipid-transfer protein likely operating at the ER-autophagosome interface. ATG2A can bind tens of glycerophospholipids at once and transfers lipids robustly in vitro.

2024年4月16日 · In this study, we identified a new ATG2A-binding protein, ANKFY1. Depletion of this endosome-localized protein led to the impaired autophagosome growth and the reduced autophagy flux, which...

2025年2月20日 · Depletion of both Atg2A and Atg2B causes clustering of enlarged lipid droplets in an autophagy-independent manner. These data suggest that mammalian Atg2 proteins function both in autophagosome formation and regulation of lipid droplet morphology and dispersion.

2019年8月26日 · We recently demonstrated that human ATG2A transfers lipids between membranes in vitro, which led us to propose a model that the phagophore expands upon the transfer of lipids from the ER by ATG2. Here, we summarize our findings and arising issues that need to be addressed to establish the mechanism of phagophore expansion.

2025年3月21日 · Additionally, molecular dynamics simulations were employed to investigate the mechanism by which ATG2A mediates lipid extraction from donor membranes. Our findings offer structural and mechanistic insights into the spatially coupled processes of lipid transfer and re-equilibration, which are essential for phagophore membrane expansion.

ATG2A in autophagosome formation, our findings reveal a previously unknown regulatory mechanism of lipid transfer proteins in cells. Results ATG2A undergoes depalmitoylation at its C-terminal during cell starvation Research conducted on yeast has demonstrated that Atg2 serves as a phosphorylation substrate for Atg1, although it is unlikely that

Here, we report the identification and characterization of mammalian Atg2 homologues Atg2A and Atg2B. Simultaneous silencing of Atg2A and Atg2B causes a block in autophagic flux and accumulation of unclosed autophagic structures containing most Atg proteins. Atg2A localizes on the autophagic membrane, as well as on the surface of lipid droplets.