2011 Fiscal Year Final Research Report
Mechanisms for switching off of CaM-kinases and their involvement in regulation of the cellular phosphorylation balance
| Project/Area Number |
21590334
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Hiroshima University |
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Principal Investigator |
ATSUHIKO Ishida 広島大学, 大学院・総合科学研究科, 准教授 (90212886)
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| Co-Investigator(Kenkyū-buntansha) |
TAKESHI Yamazaki 広島大学, 大学院・総合科学研究科, 教授 (30192397)
TATSUO Nehira 広島大学, 大学院・総合科学研究科, 助教 (60321692)
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| Co-Investigator(Renkei-kenkyūsha) |
TAKAO Mukuda 広島大学, 大学院・総合科学研究科, 助教 (60346335)
ISAMU Kameshita 香川大学, 農学部, 教授 (60127941)
NORIYUKI Sueyoshi 香川大学, 農学部, 准教授 (90346635)
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| Project Period (FY) |
2009 – 2011
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| Keywords | 分子病態学 |
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| Research Abstract |
To clarify intracellular dynamics and physiological significance of CaM-kinase phosphatse(CaMKP/ PPM1F) and its nuclear homolog, CaMKP-N(PPM1E), which had been identified as protein phosphatases involved in negative regulation of multifunctional CaM-kinases, we carried out functional analyses of these enzymes using zebrafish as a model system. These in vitro and in vivo studies revealed that CaMKP plays a pivotal role in embryogenesis of zebrafish, and that processing of CaMKP-N regulates its catalytic activity and subcellular localization.
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[Journal Article] A minimum size homologue of Ca^<2+>/ calmodulin-dependent protein kinaseIV naturally occurring in zebrafish2010
Author(s)
Nimura, T., Sugiyama, Y., Sueyoshi, N., Shigeri, Y., Ishida, A., Kameshita, I.
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Journal Title
J. Biochem
Volume: 147
Pages: 857-865
DOI
Peer Reviewed
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