Analysis of acquisition process of tyrosine kinase during eykaryotic evolution.
Project/Area Number |
24510307
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Multi-year Fund |
Section | 一般 |
Research Field |
Living organism molecular science
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Research Institution | Toho University |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2016-03-31
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Project Status |
Completed (Fiscal Year 2015)
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Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2015: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2014: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
|
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.
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Report
(5 results)
Research Products
(17 results)
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[Journal Article] Implications of expansin-like 3 gene in Dictyostelium morphogenesis.2015
Author(s)
Kawata, T., Nakamura, Y., Saga, Y., Iwade, Y., Ishikawa, M., Sakurai, A. and Shimada, N.
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Journal Title
SpringerPlus
Volume: 4
Issue: 1
Pages: 190-190
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] Two Dictyostelium tyrosine kinase-like kinases function in parallel, stress-induced STAT activation pathways.2014
Author(s)
Araki, T., Vu, L.H. Sasaki, N., Kawata, T., Eichinger, L. and Williams, J.G.
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Journal Title
Molecular Biology of the Cell
Volume: 25
Issue: 20
Pages: 3222-3233
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Presentation] Analyses of DrkA kinase in STATa activation.2015
Author(s)
Saga, Y., Iwade, Y., Ishikawa, M., Araki, T., Williams, J.G. and Kawata, T.
Organizer
Dicty 2015 Annual International Dictyostelium Conference
Place of Presentation
London, UK
Year and Date
2015-08-11
Related Report
Int'l Joint Research
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[Presentation] Dissection of the Dictyostelum STATc activation pathways.
Author(s)
Araki, T., Hai, L.V., Sasaki, N., Na, J., Kawata, T., Eichinger, L. and Williams, J.G.
Organizer
International Dictyostelium Conference
Place of Presentation
Madrid, Spain
Related Report
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