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

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Title: Structure of Atg5.Atg16, a complex essential for autophagy.
Authors: Matsushita, Minako Browse this author
Suzuki, Nobuo N. Browse this author
Obara, Keisuke Browse this author
Fujioka, Yuko Browse this author
Ohsumi, Yoshinori Browse this author
Inagaki, Fuyuhiko Browse this author
Issue Date: 2-Mar-2007
Publisher: American Society for Biochemistry and Molecular Biology
Journal Title: Journal of Biological Chemistry
Volume: 282
Issue: 9
Start Page: 6763
End Page: 6772
Publisher DOI: 10.1074/jbc.M609876200
PMID: 17192262
Abstract: 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
Type: article (author version)
Appears in Collections:薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 稲垣 冬彦

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