期刊
AUTOPHAGY
卷 16, 期 3, 页码 575-583出版社
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2019.1639300
关键词
ATG9; autophagosome; autophagy; cryo-electron microscopy; single particle
类别
资金
- Research Grants Council of Hong Kong [14105517, C4011-14R, C4012-16E, C4002-17G, AoE/M-05/12]
- National Natural Science Foundation of China [31670179, 91854201]
- CUHK Faculty Strategic Development
- Research Committee of CUHK [4053182]
Macroautophagy/autophagy is an essential process for the maintenance of cellular homeostasis by recycling macromolecules under normal and stress conditions. ATG9 (autophagy related 9) is the only integral membrane protein in the autophagy core machinery and has a central role in mediating autophagosome formation. In cells, ATG9 exists on mobile vesicles that traffic to the growing phagophore, providing an essential membrane source for the formation of autophagosomes. Here we report the three-dimensional structure of ATG9 from Arabidopsis thaliana at 7.8 angstrom resolution, determined by single particle cryo-electron microscopy. ATG9 organizes into a homotrimer, with each protomer contributing at least six transmembrane alpha-helices. At the center of the trimer, the protomers interact via their membrane-embedded and C-terminal cytoplasmic regions. Combined with prediction of protein contacts using sequence co-evolutionary information, the structure provides molecular insights into the ATG9 architecture and testable hypotheses for the molecular mechanism of autophagy progression regulated by ATG9.
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