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-Structure paper
タイトル | Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery. |
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ジャーナル・号・ページ | Cell Rep, Vol. 31, Issue 13, Page 107837, Year 2020 |
掲載日 | 2020年6月30日 |
著者 | Carlos M Guardia / Xiao-Feng Tan / Tengfei Lian / Mitra S Rana / Wenchang Zhou / Eric T Christenson / Augustus J Lowry / José D Faraldo-Gómez / Juan S Bonifacino / Jiansen Jiang / Anirban Banerjee / |
PubMed 要旨 | 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 ...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-Å 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. |
リンク | Cell Rep / PubMed:32610138 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.8 - 2.9 Å |
構造データ | EMDB-21874, PDB-6wqz: EMDB-21876, PDB-6wr4: EMDB-21877: EMDB-21878: |
化合物 | ChemComp-LMN: |
由来 |
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キーワード | MEMBRANE PROTEIN / TG9A / autophagosome / autophagy / cryoEM / molecular dynamics / transmembrane protein / membranecurvature / cellular compartments / membrane morphology / lipids |