National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM092740, DP2EB020402
United States
European Research Council (ERC)
670821
European Union
Citation
Journal: Proc Natl Acad Sci U S A / Year: 2018 Title: Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex. Authors: Saikat Chowdhury / Chinatsu Otomo / Alexander Leitner / Kazuto Ohashi / Ruedi Aebersold / Gabriel C Lander / Takanori Otomo / 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 ...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.
History
Deposition
Aug 21, 2017
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Header (metadata) release
Sep 6, 2017
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Map release
Sep 6, 2017
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Update
Jan 29, 2020
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Current status
Jan 29, 2020
Processing site: RCSB / Status: Released
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