2010 Fiscal Year Final Research Report
Molecular Mechanism and Diversity of Autophagy
| Project/Area Number |
19002015
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| Research Category |
Grant-in-Aid for Specially Promoted Research
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| Allocation Type | Single-year Grants |
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| Review Section |
Biological Sciences
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| Research Institution | Tokyo Institute of Technology (2009-2011)
National Institute for Basic Biology (2007-2008) |
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Principal Investigator |
OHSUMI Yoshinori 東京工業大学, フロンティア研究機構, 特任教授 (30114416)
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| Co-Investigator(Renkei-kenkyūsha) |
NAKATOGAWA Hitoshi 東京工業大学, フロンティア研究機構, 特任准教授 (90414010)
SUZUKI Kuninori 東京工業大学, フロンティア研究機構, 特任助教 (20373194)
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| Project Period (FY) |
2007 – 2010
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| Keywords | オートファジー / ATG / タンパク質分解 / ユピキチン様タンパク質 / 膜動態 |
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| Research Abstract |
Atg17, Atg29 and Atg31 form a stable ternary complex. Upon starvation Atg1-Atg13 joins to the complex and acts as a scaffold complex for the PAS. Other Atg proteins sequentially join to the PAS in a hierarchical manner. Using in vitro systems, we elucidated functions of the products of ubiquitin-like conjugation reactions, Atg8-PE and Atg12-Atg5. We studied selective degradation of mitochondria and identified an essential receptor, Atg32, which localizes on the mitochondrial outer membrane. Crystal structures of the most Atg proteins involved in the conjugation systems were determined.
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