Functional analysis of phosphatidylinositol 5-kinases (PIP5K)
| Project/Area Number |
11680624
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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 |
Functional biochemistry
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| Research Institution | The University of Tokyo |
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Principal Investigator |
SHIBASAKI Yoshikazu Faculty of Medicine, The University of Tokyo Assistant, 医学部・附属病院, 助手 (80196419)
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| Co-Investigator(Kenkyū-buntansha) |
KAJIO Hiroshi Faculty of Medicine, The University of Tokyo Research Fellow, 医学部・附属病院, 医員
KATAGIRI Hideki Faculty of Medicine, The University of Tokyo Research Fellow, 医学部・附属病院, 医員
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| Project Period (FY) |
1999 – 2000
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| Project Status |
Completed (Fiscal Year 2001)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,900,000)
Fiscal Year 2000: ¥1,100,000 (Direct Cost: ¥1,100,000)
Fiscal Year 1999: ¥2,800,000 (Direct Cost: ¥2,800,000)
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| Keywords | inositol / kinase / actin / low molecular weight G protein / membrane traffic / vesicular transport / cytoskeleton / キナーゼ / ホスホリパーゼD / PHドメイン / ラフリング |
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| Research Abstract |
(1) Analysis of mutant PIP5K : By deleting either N-terminus or C-terminus, the kinase activity of PIP5K was localized in central 380 amino acids region.
(2) Intracellular localization of PIP5K : Endogenous PIP5K was hard to detect as the expression was very low. Exogenous PIP5K was found mainly on the cytoplasmic surface of the plasma membrane and also in the cytoplasm.
(3) Products of PIP5K reaction : In addition to PI (4,5) P2, small amount of PI (5) P and PI (3,5) P2 was produced.
(4) Actin polymerization : By overexpression of PIP5K, actin polymerization was greatly enhanced.
(5) Interactin between Rac and PIP5K : In platelet semiintact system, Rac and PIP5K are both involved in thrombin stimulated actin polymerization process. When a Rac mutant was introduced, the polymerization was inhibited, suggesting that the interaction between Rac and PIP5K is necessary for actin polymerization
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Report
(3 results)
Research Products
(11 results)
