Analysis of acquisition process of tyrosine kinase during eykaryotic evolution.

2015 Fiscal Year Final Research Report

• Project/Area Number: 24510307
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Living organism molecular science
• Research Institution: Toho University
• Principal Investigator: KAWATA Takefumi 東邦大学, 理学部, 教授 (30221899)
• Project Period (FY): 2012-04-01 – 2016-03-31
• Keywords: チロシンキナーゼ / シグナル伝達 / 転写因子 / SH2ドメイン / 細胞性粘菌 / チロシンキナーゼ様タンパク質

Outline of Final Research Achievements

Social amoeba, Dictyostelium discoideum, harbors a number of tyrosine kinase-like kinases (TKLs). In this project, we analyzed three TKLs, DrkA, DrkC and RckA, that may phosphorylate tyrosine residue on a transcription factor STATa. We created a strain with a mutation of all three genes. The phosphorylation of the STATa was almost abolished in the mutant strain using a buffered artificial phosphorylation induction experiment. This indicates these TKLs play vital roles for STATa phosphorylation. However, STATa was phosphorylated in the mutant strain when it developed into a multicellular stage. Although we cannot explain this paradox at the moment, if the function of any particular TKL is inactivated then other TKL including unidentified novel one might replace it to show redundancy. To elucidate the redundancy mechanism would help to understand the new insights into evolutional acquisition process of protein tyrosine kinase.

Free Research Field

分子発生生物学