The novel molecular recognition mechanism of Ras by its structural polymorphism

2016 Fiscal Year Final Research Report

• Project/Area Number: 25871145
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics; Structural biochemistry
• Research Institution: Institute of Physical and Chemical Research
• Principal Investigator: Nobuhisa Umeki 国立研究開発法人理化学研究所, 佐甲細胞情報研究室, 研究員 (70647502)
• Project Period (FY): 2013-04-01 – 2017-03-31
• Keywords: Ras / RalGDS / 1分子計測 / 細胞内情報伝達

Outline of Final Research Achievements

To understand the mechanism of Ras-RalGDS-Ral signaling, translocation dynamics of RalGDS and its functional domains (RBD and REMCDC) to the plasma membranes of living cells were measured. Although the RBD played an important role in increasing the association rate constant between RalGDS and the plasma membrane, the REMCDC domain affected the dissociation rate constant from the membrane, which decreased after Ras activation. Thus, multiple regions and domains of both Ras and RalGDS work concertedly to regulate the Ras-RalGDS-Ral signaling. It is also suggested that the structural polymorphism of Ras is involved in interaction of Ras and RalGDS.

Free Research Field

生物物理学、生化学、細胞生物学