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• W2890848016 abstract "Autophagy is an enigmatic cellular process in which double-membrane compartments, called “autophagosomes, form de novo adjacent to the endoplasmic reticulum (ER) and package cytoplasmic contents for delivery to lysosomes. Expansion of the precursor membrane phagophore requires autophagy-related 2 (ATG2), which localizes to the PI3P-enriched ER–phagophore junction. We combined single-particle electron microscopy, chemical cross-linking coupled with mass spectrometry, and biochemical analyses to characterize human ATG2A in complex with the PI3P effector WIPI4. ATG2A is a rod-shaped protein that can bridge neighboring vesicles through interactions at each of its tips. WIPI4 binds to one of the tips, enabling the ATG2A-WIPI4 complex to tether a PI3P-containing vesicle to another PI3P-free vesicle. These data suggest that the ATG2A-WIPI4 complex mediates ER–phagophore association and/or tethers vesicles to the ER–phagophore junction, establishing the required organization for phagophore expansion via the transfer of lipid membranes from the ER and/or the vesicles to the phagophore." @default.
• W2890848016 created "2018-09-27" @default.
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• W2890848016 date "2018-09-05" @default.
• W2890848016 modified "2023-10-16" @default.
• W2890848016 title "Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex" @default.
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• W2890848016 doi "https://doi.org/10.1073/pnas.1811874115" @default.
• W2890848016 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6196511" @default.
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