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Structure of Atg5.Atg16, a complex essential for autophagy.

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タイトル: Structure of Atg5.Atg16, a complex essential for autophagy.
著者: Matsushita, Minako 著作を一覧する
Suzuki, Nobuo N. 著作を一覧する
Obara, Keisuke 著作を一覧する
Fujioka, Yuko 著作を一覧する
Ohsumi, Yoshinori 著作を一覧する
Inagaki, Fuyuhiko 著作を一覧する
発行日: 2007年 3月 2日
出版者: American Society for Biochemistry and Molecular Biology
誌名: Journal of Biological Chemistry
巻: 282
号: 9
開始ページ: 6763
終了ページ: 6772
出版社 DOI: 10.1074/jbc.M609876200
抄録: Atg5 is covalently modified with a ubiquitin-like modifier, Atg12, and the Atg12-Atg5 conjugate further forms a complex with the multimeric protein Atg16. The Atg12-Atg5·Atg16 multimeric complex plays an essential role in autophagy, the bulk degradation system conserved in all eukaryotes. We have reported here the crystal structure of Atg5 complexed with the N-terminal region of Atg16 at 1.97Å resolution. Atg5 comprises two ubiquitin-like domains that flank a helix-rich domain. The N-terminal region of Atg16 has a helical structure and is bound to the groove formed by these three domains. In vitro analysis showed that Arg-35 and Phe-46 of Atg16 are crucial for the interaction. Atg16, with a mutation at these residues, failed to localize to the pre-autophagosomal structure and could not restore autophagy in Atg16-deficient yeast strains. Furthermore, these Atg16 mutants could not restore a severe reduction in the formation of the Atg8-phosphatidylethanolamine conjugate, another essential factor for autophagy, in Atg16-deficient strains under starvation conditions. These results taken together suggest that the direct interaction between Atg5 and Atg16 is crucial to the performance of their roles in autophagy.
Rights: Copyright © 2007 by the American Society for Biochemistry and Molecular Biology
資料タイプ: article (author version)
URI: http://hdl.handle.net/2115/22079
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 稲垣 冬彦

 

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