| Project/Area Number |
24650204
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Single-year Grants |
|---|
| Research Field |
Neurochemistry/Neuropharmacology
|
|---|
| Research Institution | Institute of Physical and Chemical Research |
|---|
Principal Investigator |
SANEYOSHI Takeo 独立行政法人理化学研究所, 脳科学総合研究センター, 研究員 (00556201)
|
|---|
| Project Period (FY) |
2012-04-01 – 2014-03-31
|
| Project Status |
Completed (Fiscal Year 2013)
|
| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
|
|---|
| Keywords | シナプス / CaMKII / 酵素 / 非天然アミノ酸 / 基質 / リン酸化 / シナプス可塑性 / 酵素反応 / プロテオミクス |
|---|
| Research Abstract |
It is widely accepted that Calmodulin-kinase II (CaMKII) plays important roles in learning and memory. Although plasticity of synapse regulated by CaMKII, direct targets of CaMKII has poorly identified. To obtain cellular CaMKII substrates, we tried to apply unnatural amino acid incorporation method. Several phenylalanine residues in catalytic domain of CaMKII were made for subsequent incorporation of an unnatural amino acid pBpa. The pBpa were successfully incorporated on CaMKII in HEK293 cells. The covalent bonds were formed upon UV irradiation in cells expressing CaMKII mutants, especially residues, F16, F157, F171. This mutants are useful molecules to identify cellular substrate for CaMKII.
|
