Journal
CELL REPORTS
Volume 31, Issue 13, Pages -Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2020.107837
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Funding
- Intramural Research Program of the National Heart, Lung, and Blood Institute, National Institutes of Health
- Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health [ZIA HD001607, ZIA HD008928]
- EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT [ZIAHD008928, ZIAHD001607] Funding Source: NIH RePORTER
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [ZIAHL006203, ZIAHL006238] Funding Source: NIH RePORTER
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Autophagy is a catabolic process involving capture of cytoplasmic materials into double-membraned autophagosomes that subsequently fuse with lysosomes for degradation of the materials by lysosomal hydrolases. One of the least understood components of the autophagy machinery is the transmembrane protein ATG9. Here, we report a cryoelectron microscopy structure of the human ATG9A isoform at 2.9-angstrom resolution. The structure reveals a fold with a homotrimeric domain-swapped architecture, multiple membrane spans, and a network of branched cavities, consistent with ATG9A being a membrane transporter Mutational analyses support a role for the cavities in the function of ATG9A. In addition, structure-guided molecular simulations predict that ATG9A causes membrane bending, explaining the localization of this protein to small vesicles and highly curved edges of growing autophagosomes.
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