Elucidation of attenuation system for autophagy by phosphatases

2015 Fiscal Year Final Research Report

• Project/Area Number: 25460063
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Biological pharmacy
• 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): 2013-04-01 – 2016-03-31
• 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

Outline of Final Research Achievements

Autophagy is a conserved eukaryotic process of vacuolar/lysosomal-mediated degradation targeting proteins and organelles. Autophagy has to be tightly regulated in order to prevent its occurring at insufficient or excess levels, both of which are harmful for cells. So far, the regulation of autophagy by phosphorylation catalyzed by kinases have been primarily investigated; however, the importance of its reverse reaction, catalyzed by phosphatases, needs to be elucidated.
In this study, I demonstrate that two phosphatases, PP2A and calcineurin, are required for dephosphorylation of Atg13 upon autophagy induction and that Msg5 and Sdp1 dephosphorylate Slt2 kinase to suppress autophagy. In addition, I identified a novel component of the PI3 kinase complex, Atg38. Atg38 functions as a physical linkage between the Vps15-Vps34 and Atg14-Vps30 sub-complexes to facilitate complex I formation.

Free Research Field

細胞生物学