Establishment of a method for identification of ubiquitin ligase substrates in eukaryotic cells by application of bacterial ubiquitin-like modifier Pup

2021 Fiscal Year Final Research Report

• Project/Area Number: 20K21401
• Research Category: Grant-in-Aid for Challenging Research (Exploratory)
• Allocation Type: Multi-year Fund
• Review Section: Medium-sized Section 43:Biology at molecular to cellular levels, and related fields
• Research Institution: University of Miyazaki
• Principal Investigator: Nishitoh Hideki 宮崎大学, 医学部, 教授 (00332627)
• Project Period (FY): 2020-07-30 – 2022-03-31
• Keywords: タンパク質分解

Outline of Final Research Achievements

Understanding the proteolytic system is an important research issue, as failure of the proteolytic system leads to the accumulation of defective proteins and the development of conformational diseases such as neurodegenerative disorders. The principal investigator has promoted research on proteolysis, which is necessary for quality control of the endoplasmic reticulum. In proteolysis, "Is there specificity in the ubiquitination of defective proteins to be degraded?" If so, what is the law of specificity? If so, what is the law of specificity?" We have developed a novel method to identify ubiquitination substrates to solve these questions.

Free Research Field

細胞生物学

Academic Significance and Societal Importance of the Research Achievements

本手法の確立によって、小胞体におけるタンパク質分解に関与するユビキチンリガーゼの基質を同定することに成功した。本手法の獲得は、理論上全てのE3に応用可能である。今後は、真核細胞での網羅的解析により、タンパク質分解だけでなく新規シグナル伝達経路の発見にも繋がると期待される。