• Search Research Projects
  • Search Researchers
  • How to Use
  1. Back to project page

2014 Fiscal Year Final Research Report

Mechanisms of protein disulfide bond formation in the ER of mammalian cells

Research Project

  • PDF
Project/Area Number 24580141
Research Category

Grant-in-Aid for Scientific Research (C)

Allocation TypeMulti-year Fund
Section一般
Research Field Applied biochemistry
Research InstitutionTohoku University (2013-2014)
Nara Institute of Science and Technology (2012)

Principal Investigator

KADOKURA Hiroshi  東北大学, 多元物質科学研究所, 准教授 (70224558)

Co-Investigator(Renkei-kenkyūsha) SAITO Michiko  奈良先端科学技術大学院大学, バイオサイエンス研究科, 助教 (40379558)
KOHNO Kenji  奈良先端科学技術大学院大学, バイオサイエンス研究科, 教授 (50142005)
Project Period (FY) 2012-04-01 – 2015-03-31
Keywords物質生産 / ジスルフィド結合 / 立体構造形成 / 分泌タンパク質 / 小胞体 / 哺乳動物
Outline of Final Research Achievements

Formation of disulfide bonds is a crucial step in the folding of a number of proteins that go through the secretory pathway. They include proteins with industrial importance such as insulin. The ER of mammalian cells harbors twenty enzymes that belong to thioredoxin-superfamily members (they are also called thioredoxin-like proteins). These enzymes are implicated in the formation of protein disulfide bonds. However, the physiological function of each enzyme is unclear, due to the lack of information on its substrates. To gain insights into the role of JPDI, one of the enzymes, we successfully identified the potential substrates of this enzyme from a mouse tissue. Furthermore, we were able to identify four of thioredoxin-superfamily members that interacted with proinsulin (a precursor of insulin) via formation of an intermolecular disulfide bond. These findings provide insights into the mechanisms of folding of secretory proteins in mammalian cells.

Free Research Field

農学

URL: 

Published: 2016-06-03  

Information User Guide FAQ News Terms of Use Attribution of KAKENHI

Powered by NII kakenhi