期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 21, 期 6, 页码 513-521出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2822
关键词
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资金
- Japan Society for the Promotion of Sciences KAKENHI [24113725, 25111004, 2440279, 30114416, 24770182]
- Targeted Proteins Research Program from the Ministry of Education, Culture, Sports, Science and Technology of Japan
- Grants-in-Aid for Scientific Research [23000015, 22121008, 24770182, 24113725, 12J08262, 25111004, 26111508] Funding Source: KAKEN
Assembly of the preautophagosomal structure (PAS) is essential for autophagy initiation in yeast. Starvation-induced dephosphorylation of Atg13 is required for the formation of the Atg1-Atg13-Atg17-Atg29-Atg31 complex (Atg1 complex), a prerequisite for PAS assembly. However, molecular details underlying these events have not been established. Here we studied the interactions of yeast Atg13 with Atg1 and Atg17 by X-ray crystallography. Atg13 binds tandem microtubule interacting and transport domains in Atg1, using an elongated helix-loop-helix region. Atg13 also binds Atg17, using a short region, thereby bridging Atg1 and Atg17 and leading to Atg1-complex formation. Dephosphorylation of specific serines in Atg13 enhanced its interaction with not only Atg1 but also Atg17. These observations update the autophagy-initiation model as follows: upon starvation, dephosphorylated Atg13 binds both Atg1 and Atg17, and this promotes PAS assembly and autophagy progression.
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