Study on the protein quality control mechanism in the endoplasmic reticulum

2016 Fiscal Year Final Research Report

• Project/Area Number: 26440096
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Cell biology
• Research Institution: Kyoto University
• Principal Investigator: Hosokawa Nobuko 京都大学, ウイルス・再生医科学研究所, 准教授 (00263153)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: 小胞体 / タンパク質品質管理 / シャペロンタンパク質 / タンパク質分解 / 小胞体関連分解 / 動物細胞

Outline of Final Research Achievements

Newly synthesized proteins obtain its native conformations by the assistance of chaperone proteins and folding enzymes, while polypeptides that failed to fold correctly are disposed by the intracellular degradation machinery. This mechanism is named as protein quality control. Misfolded proteins are prone to aggregate, and accumulation of these abnormal species frequently impairs cellular function, causing conformational diseases.
In the present study, we analyzed the molecular mechanisms of protein quality control system in mammalian endoplasmic reticulum (ER), focusing on the proteins that inhibit aggregation formation in the ER, and the membrane complex in the ER that plays the central role in ER-associated protein degradation.

Free Research Field

細胞生物学