2016 Fiscal Year Final Research Report
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 |
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| Section | 一般 |
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| Research Field |
Functional biochemistry
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| Research Institution | Okayama University |
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Principal Investigator |
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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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| Keywords | CaMKK / AMPK / STO-609 / CaMK cascade / Protein Kinase / Signal Transduction |
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| 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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| Free Research Field |
生化学
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