Clarification of the mechanisms of new signal transductions at the downstram of small GTPase, Rho protein.
| Project/Area Number |
12670120
|
|---|
| Research Category |
Grant-in-Aid for Scientific Research (C)
|
| Allocation Type | Single-year Grants |
|---|
| Section | 一般 |
|---|
| Research Field |
General medical chemistry
|
|---|
| Research Institution | Foundation for Advancement of International Science (2001)
Dokkyo Medical University (2000) |
|---|
Principal Investigator |
TOMOKO Tominaga Foundation for Advancement of International Science, Investigator, 研究開発部, 専任研究員 (00280587)
|
|---|
| Co-Investigator(Kenkyū-buntansha) |
白瀧 博通 獨協医科大学, 医学部, 教授 (90249962)
|
|---|
| Project Period (FY) |
2000 – 2001
|
| Project Status |
Completed (Fiscal Year 2001)
|
| Budget Amount *help |
¥3,400,000 (Direct Cost: ¥3,400,000)
Fiscal Year 2001: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 2000: ¥2,000,000 (Direct Cost: ¥2,000,000)
|
|---|
| Keywords | Rho / mDia / DIP / Src / cell movement / cell adhesion / 軸索伸長 / Grb2 |
|---|
| Research Abstract |
The aim of this project is to clarify the mechanism of cell movement from the aspects of intracellular signaling events occurred by small GTPase Rho family proteins and cell adhesion molecules. Currently, my proposal project is focusing on the signaling events occurred by mDia (mammalian Diaphanous), which belongs to the formin homology protein family essential for cytokinesis.
I found two new signal pathways in the downstream of Rho, Rho-mDia-Src pathway (Ref. 1) and mDia-DIP-Grb2 one (Ref. 2). DIP is a new mDia interacting protein which is expressed ubiquitously and has several unique domains. DIP mainly binds to the proline rich region of mDia (FH1) through its fyn-like SH3 domain, and also binds to Grb2 through its proline-rich domain. DIP is localized at the cell periphery and membrane ruffles, and co-localizes with mDia. Co-expression of vSrc and DIP induces significant morphological changes at focal contacts and activation of vSrc.
The turnover of focal contacts is occurred by co-ordination with focal adhesion molecules, including Src and Rho signaling-related substances. Therefore, I continue to investigate the role of mDia-Src and DIP pathways in the turnover of focal contacts.
|
Report
(3 results)
Research Products
(9 results)
-
-
-
-
-
-
-
[Publications] Tominaga, T., Sahai, E., Chardin, P., McCormick, F., Courtneidge, SA., Alberts, AS: "Diaphanous -related formines bridge Rho GTPases and Src tyrosine kinase signaling"Mol. Cell. 5. 13-25 (2000)
-
-
