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TitleStructure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery.
Journal, issue, pagesCell Rep, Vol. 31, Issue 13, Page 107837, Year 2020
Publish dateJun 30, 2020
AuthorsCarlos 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 AbstractAutophagy 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.
External linksCell Rep / PubMed:32610138 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 2.9 Å
Structure data

21874

6wqz

EMDB-21874, PDB-6wqz:
Structure of human ATG9A, the only transmembrane protein of the core autophagy machinery
Method: EM (single particle) / Resolution: 2.8 Å

21876

6wr4

EMDB-21876, PDB-6wr4:
Structure of human ATG9A, the only transmembrane protein of the core autophagy machinery
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-21877:
ATG9A stateA monomer map
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-21878:
ATG9A stateB monomer
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-LMN:
Lauryl Maltose Neopentyl Glycol / detergent*YM

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / TG9A / autophagosome / autophagy / cryoEM / molecular dynamics / transmembrane protein / membranecurvature / cellular compartments / membrane morphology / lipids

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