Studies on regulation of autophagosome formation by kinases andphosphatases
Project/Area Number |
23890059
|
Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Biological pharmacy
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Research Institution | Tokyo Institute of Technology |
Principal Investigator |
ARAKI Yasuhiro 東京工業大学, フロンティア研究機構, 特任助教 (60345254)
|
Project Period (FY) |
2011 – 2012
|
Project Status |
Completed (Fiscal Year 2012)
|
Budget Amount *help |
¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
Keywords | オートファジー / リン酸化 / キナーゼ / ホスファターゼ / 蛋白質分解 / 酵母 / PI3キナーゼ / Vps34 / Atg14 / 蛋白質 / 細胞 / シグナル伝達 / 脂質 / ストレス |
Research Abstract |
Autophagy is a conserved eukaryotic process of vacuolar/lysosomal-mediated degradation targeting proteins and organelles. Autophagy is characterized by the formation of a cytosolic double-membrane structure, the autophagosome. The molecular mechanisms underlying the process of autophagy remain to be elucidated. Here, I demonstrate that Atg1 kinase, the substrates of which were unknown, phosphorylates Atg13 and Vps34. In addition, I identify a novel component of the PI3 kinase complex, Atg38. Atg38 is required for the integrity of this complex.
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Report
(3 results)
Research Products
(11 results)