Analysis of unidentified truncation mechanism of misfolded proteins

Research Project

Project/Area Number	25440058
Research Category	Grant-in-Aid for Scientific Research (C)
Allocation Type	Multi-year Fund
Section	一般
Research Field	Functional biochemistry
Research Institution	Institute of Physical and Chemical Research
Principal Investigator	Hosomi Akira 国立研究開発法人理化学研究所, 糖鎖代謝学研究チーム, 協力研究員 (60525864)
Project Period (FY)	2013-04-01 – 2016-03-31
Project Status	Completed (Fiscal Year 2015)
Budget Amount *help	¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000) Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000) Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000) Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Keywords	酵母 / 小胞体関連分解 / エンドペプチダーゼ / ERAD / glycoprotein / yeast / 異常タンパク質 / タンパク質分解
Outline of Final Research Achievements	Misfolded proteins are degraded by proteasome in ER-associated degradation (ERAD). However, our previous study suggested that unidentified protease cleaves CPY* (carboxypeptidase Y mutant), which is a major ERAD model substrate, in budding yeast. To clarify the mechanism of the cleavage, we analyzed CPY* intermediates. Our study demonstrated that 50k and 30k intermediates were generated and cleavage site for 50k intermediate is located in 400-404 amino acid residues.

Report

(4 results)