Elucidation of cellular functions by myristoylation-dependent protein-protein interaction
| Project/Area Number |
24580150
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Multi-year Fund |
|---|
| Section | 一般 |
|---|
| Research Field |
Applied biochemistry
|
|---|
| Research Institution | Kyoto Gakuen University |
|---|
Principal Investigator |
|
|---|
| Project Period (FY) |
2012-04-01 – 2015-03-31
|
| Project Status |
Completed (Fiscal Year 2014)
|
| Budget Amount *help |
¥5,590,000 (Direct Cost: ¥4,300,000、Indirect Cost: ¥1,290,000)
Fiscal Year 2014: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2013: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
|
|---|
| Keywords | ミリスチル化 / ミリストイル化 / 脂質修飾 / シグナル伝達 / 蛋白質間相互作用 / リン酸化 / 転写抑制因子 / 核移行 |
|---|
| Outline of Final Research Achievements |
A variety of oncogene and signal transduction proteins are known to be myristoylated. Although the role of myristoylation in protein-lipid interaction is well established, the involvement of myristoylation in protein-protein interaction is less well understood.
To elucidate the myristoylation-dependent protein-protein interaction, we detected the binding proteins of NAP22 in a miyristoyaltion-dependent manner. The binding proteins included the nuclear proteins such as HMGB1. Protein-protein interactions of HMGB1 and myristoylated NAP-22 were observed in cytosol and nuclear regions of various mammalian cells. These results suggest that myristoylation-dependent protein-protein interaction might be very significant to cellular function.
|
Report
(4 results)
Research Products
(10 results)
-
[Journal Article] Partial Purification and Characterization of the Rat Parotid Gland Protein Kinase Catalyzing Phosphorylation of Matures Destrin at Ser-2.2014
Author(s)
Osumi, E., Kondo, C., Mizuno, M., Suzuki, T. Matsubara, M., Shimozato, K. and Kanamori, T.
-
Journal Title
Advances in Enzyme Research
Volume: 2
Issue: 02
Pages: 100-112
DOI
Related Report
Peer Reviewed / Open Access
-
-
-
-
-
-
-
-
-
