| First Author | Lopez-Ilasaca MA | Year | 2005 |
| Journal | FEBS Lett | Volume | 579 |
| Issue | 3 | Pages | 648-54 |
| PubMed ID | 15670823 | Mgi Jnum | J:122694 |
| Mgi Id | MGI:3715074 | Doi | 10.1016/j.febslet.2004.12.039 |
| Citation | Lopez-Ilasaca MA, et al. (2005) Bioluminescence resonance energy transfer identify scaffold protein CNK1 interactions in intact cells. FEBS Lett 579(3):648-54 |
| abstractText | Connector enhancer of KSR (CNK) proteins have been proposed to act as scaffolds in the Ras-MAPK pathway. In this work, using in vivo bioluminescence resonance energy transfer (BRET) assays and in vitro co-immunoprecipitation, we show that hCNK1 interacts with the active form of Rho A (G14V) proteins. The domain of hCNK1 that allows binding to Rho proteins involves the C-terminal PH domain. Overexpression of hCNK1 does not affect the actin cytoskeleton and does not modify the appearance of stress fibers in cells overexpressing a constitutively active form of RhoA. In contrast, hCNK1 was able to significantly decrease the RhoA-induced transcriptional activity of the serum response element (SRE) without effect on the Ras-induced SRE activation. These results identify hCNK1 as a specific partner of Rho proteins both in vitro and in vivo and suggest a role of hCNK1 in the signal transduction of Rho proteins. |
