Molecular basis of new protein quality control systems depending on the pH gradient between the ER and the Golgi

2017 Fiscal Year Final Research Report

• Project/Area Number: 15H04335
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Tohoku University
• Principal Investigator: Inaba Kenji 東北大学, 多元物質科学研究所, 教授 (10423039)
• Project Period (FY): 2015-04-01 – 2018-03-31
• Keywords: タンパク質品質管理 / 小胞体 / ゴルジ体 / Ｘ線結晶構造解析 / ERp44 / PDIファミリー

Outline of Final Research Achievements

ERp44 is a PDI-family member protein that transports back ER-resident enzymes and immature secretory proteins from the Golgi to the ER and thereby conducts protein quality control in the early secretory pathway. In this reserach project, we succeeded in crystal structure analysis of ERp44 at pH7.5 and pH6.5. Based on the structural information, we performed a series of biochemical, biophysical and cell biological studies. Consequently, we revealed the molecular mechanism by which ERp44 regulates the substrate binding and release in a pH-dependent manner (Watanabe et al., PNAS 2017).

Free Research Field

構造生物化学