2013 Fiscal Year Final Research Report

Molecular basis regulating multiple signals by an adaptor protein

Research Project

Project/Area Number	24770087
Research Category	Grant-in-Aid for Young Scientists (B)
Allocation Type	Multi-year Fund
Research Field	Structural biochemistry
Research Institution	Hokkaido University
Principal Investigator	OSE TOYOYUKI 北海道大学, 薬学研究科(研究院), 准教授 (80380525)
Project Period (FY)	2012-04-01 – 2014-03-31
Keywords	シグナル伝達
Research Abstract	The non-receptor tyrosine kinase breast tumor kinase (Brk), also known as PTK6, has been identified as a highly expressed Protein-tyrosine kinases in human melanocyte. STAP-2 is also known as breast tumor kinase (Brk) substrate (BKS). it is important to better understand the contribution of Brk kinase activity and protein interactions to the STAT3-mediated signal transduction pathways in breast cancer. Brk phosphorylates STAP-2 and phosphorylated STAP-2 is believed to play an important role in Brk-mediated STAT3 activation. We purified Brk, STAP-2, and STAT3 and checked the kinase activity in vitro. Using purified proteins, we also checked the binding affinity between Brk and STAP-2. The information obtained by small angle xray scattering (SAXS) experiments was also useful to judge whether the conformational change of Brk is included (open/closed).

(1 results)