Phosphorylation-dependent regulatory mechanism of calmoudlin-kinase cascade
Project/Area Number |
26440056
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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 |
Functional biochemistry
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Research Institution | Okayama University |
Principal Investigator |
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Co-Investigator(Kenkyū-buntansha) |
曲 正樹 岡山大学, 自然科学研究科, 助教 (50359882)
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Co-Investigator(Renkei-kenkyūsha) |
HATANO Naoya 神戸大学, 大学院医学(系)研究科, 特命助教 (10332280)
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Project Period (FY) |
2014-04-01 – 2017-03-31
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Project Status |
Completed (Fiscal Year 2016)
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Budget Amount *help |
¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2016: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2014: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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Keywords | CaMKK / AMPK / STO-609 / CaMK cascade / Protein Kinase / Signal Transduction / リン酸化反応 / AMPキナーゼ / CaMキナーゼI V / 細胞内カルシウム / シグナル伝達 / 特異性 / CaMK Cascade |
Outline of Final Research Achievements |
Intracellular Ca2+ plays an important role in the cellular signal transduction system as a second messenger. Calmodulin (caM) is one of Ca2+-binding proteins, which activates multifunctional CaM-kinases. In this research, we examined the molecular mechanism of substrate recognition for Ca2+/calmodulin-dependent protein kinase kinase beta based on the structure-function analysis.
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] Compartmentalized AMPK Signaling Illuminated by Genetically Encoded Molecular Sensors and Actuators2015
Author(s)
Miyamoto T, Rho E, Sample V, Akano H, Magari M, Ueno T, Gorshkov K, Chen M, Tokumitsu H, Zhang J, Inoue T
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Journal Title
Cell Reports
Volume: 印刷中
Issue: 4
Pages: 657-670
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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