Regulation of phospholipid metabolisms by IRBIT family
Project/Area Number |
21870049
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Research Category |
Grant-in-Aid for Research Activity Start-up
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Allocation Type | Single-year Grants |
Research Field |
Functional biochemistry
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Research Institution | The Institute of Physical and Chemical Research |
Principal Investigator |
ANDO Hideaki The Institute of Physical and Chemical Research, 発生神経生物研究チーム, 客員研究員 (50373262)
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Research Collaborator |
TAKENAWA Tadaomi 神戸大学, 医学(系)研究科(研究院), 教授 (40101315)
IJUIN Takeshi 神戸大学, 医学(系)研究科(研究院), 助教 (00361626)
ITOH Toshiki 神戸大学, 医学(系)研究科(研究院), 准教授 (30313092)
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Project Period (FY) |
2009 – 2010
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Project Status |
Completed (Fiscal Year 2010)
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Budget Amount *help |
¥2,756,000 (Direct Cost: ¥2,120,000、Indirect Cost: ¥636,000)
Fiscal Year 2010: ¥1,313,000 (Direct Cost: ¥1,010,000、Indirect Cost: ¥303,000)
Fiscal Year 2009: ¥1,443,000 (Direct Cost: ¥1,110,000、Indirect Cost: ¥333,000)
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Keywords | IRBIT / PIP2合成酵素 / イノシトールリン脂質 / タンパク質相互作用 / PIP2 / PIP kinase / IP3受容体 |
Research Abstract |
We analyzed the interaction between IRBIT/Long-IRBIT and PIP kinase family. IRBIT specifically bound to PIPKIα in mouse brain and the interaction was direct. On the contrary, Long-IRBIT did not interacted with PIPKI. The interaction between IRBIT and PIPKIα was dependent on the phosphorylation sites of IRBIT and the catalytic amino acid of PIPKIα. Furthermore, in vitro lipid kinase assay suggested the possibility that IRBIT suppresses the activity of PIPKIα.
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Report
(3 results)
Research Products
(11 results)
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[Journal Article] Inositol 1,4,5-triphosphate receptor-binding protein released with inositol 1,4,5-triphosphate (IRBIT) associates with components of the mRNA 3' processing machinery in a phosphorylation-dependent manner and inhibits polyadenylation.2009
Author(s)
Kiefer H, Mizutani A, Iemura S, Natsume T, Ando H, Kuroda Y, Mikoshiba K
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Journal Title
J.Biol.Chem. 284(16)
Pages: 10694-10705
Related Report
Peer Reviewed
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