| Autor: |
Druey, Kirk M., Waheed, Abdul A., Kreutz, Barry, Suzuki, Nobuchika, Kozasa, Tohru, Jones, Teresa L. Z., Brown, Joan Heller, Seasholtz, Tammy M., Johnson, Eric N. |
| Předmět: |
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| Zdroj: |
Nature Cell Biology; Dec2003, Vol. 5 Issue 12, p1095-1103, 9p, 5 Diagrams |
| Abstrakt: |
Ga13 stimulates the guanine nucleotide exchange factors (GEFs) for Rho, such as p115Rho-GEF. Activated Rho induces numerous cellular responses, including actin polymerization, serum response element (SRE)-dependent gene transcription and transformation. p115Rho-GEF contains a Regulator of G protein Signalling domain (RGS box) that confers GTPase activating protein (GAP) activity towards Ga12 and Ga13 (ref. 3). In contrast, classical RGS proteins (such as RGS16 and RGS4) exhibit RGS domain-dependent GAP activity on Gai and Gaq, but not Ga12 or Ga13 (ref 4). Here, we show that RGS16 inhibits Ga13-mediated, RhoA-dependent reversal of stellation and SRE activation. The RGS16 amino terminus binds Ga13 directly, resulting in translocation of Ga13 to detergent-resistant membranes (DRMs) and reduced p115Rho-GEF binding. RGS4 does not bind Ga13 or attenuate Ga13-dependent responses, and neither RGS16 nor RGS4 affects Ga12-mediated signalling. These results elucidate a new mechanism whereby a classical RGS protein regulates Ga13-mediated signal transduction independently of the RGS box. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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