Mechanism of selective substrate recognition by the ubiquitin ligase

2016 Fiscal Year Final Research Report

• Project Area: New aspect of the ubiquitin system : its enormous roles in protein regulation
• Project/Area Number: 24112006
• Research Category: Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area)
• Allocation Type: Single-year Grants
• Review Section: Biological Sciences
• Research Institution: Nagoya University
• Principal Investigator: Kamura Takumi 名古屋大学, 理学研究科, 教授 (40333455)
• Co-Investigator(Kenkyū-buntansha): 畠山 鎮次 北海道大学, 医学(系)研究科(研究院), 教授 (70294973)
• Project Period (FY): 2012-06-28 – 2017-03-31
• Keywords: ユビキチン修飾

Outline of Final Research Achievements

Ubiquitin system controls a variety of cellular processes. In this research, we try to clarify the new substrates and function of Cullin-type and TRIM-type E3s. Now we show that, in the Cullin type E3s, Ucc1, SSB4, ASB7 and Prame is related to the regulation of citric acid composition, signal transduction, spindle formation and transcription, respectively. Furthermore, we demonstrate that, in the TRIM-type E3s, TRIM45, TRIM23, TRIM29 and RNF207 controls tumor suppression, fat cell differentiation, DNA repair and glucose metabolism, respectively. Our findings shed the light on the new function of Cullin-type and TRIM-type E3s.

Free Research Field

生物学