Structural studies for specific recognition of ubiquitin signals

2016 Fiscal Year Final Research Report

• Project Area: New aspect of the ubiquitin system : its enormous roles in protein regulation
• Project/Area Number: 24112009
• 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: University of Hyogo
• Principal Investigator: MIZUSHIMA TSUNEHIRO 兵庫県立大学, 生命理学研究科, 教授 (90362269)
• Co-Investigator(Kenkyū-buntansha): 加藤 龍一 大学共同利用機関法人高エネルギー加速器研究機構, 物質構造科学研究所, 准教授 (50240833)
• Research Collaborator: KUWABARA Naoyuki ; TAKAGI Kenji
• Project Period (FY): 2012-06-28 – 2017-03-31
• Keywords: 蛋白質 / ユビキチン / 構造生物学 / 分子認識 / Ｘ線結晶構造解析

Outline of Final Research Achievements

Ubiquitin modification controls various cellular processes, such as cell cycle control and protein quality control. This modification provides countless possibilities to assemble a specific polymer. Ubiquitin modification pathway is regulated by a variety of proteins including ubiquitin binding proteins, ubiquitin ligases and deubiquitinating enzymes. To elucidate the molecular mechanisms of ubiquitination pathway, we determined the crystal structures of ubiquitin binding protein, BAG6 and ubiquitin ligases, FBG3, HOIP and Keap1. Moreover, we have determined the structures of bacterial effectors, OspI and IpaH9.8 that manipulate the host ubiquitin pathway. These structures provide the substrate recognition and functional mechanisms.

Free Research Field

構造生物学