p116Rip, originally identified as a binding partner of activated RhoA, is an actin-binding protein that interacts with the regulatory myosin-binding subunit (MBS) of myosin-II phosphatase and is essential for Rho-regulated cytoskeletal contractility. Here, we have examined the role of p116Rip in RhoA-mediated activation of the transcription factor SRF. We show that p116Rip oligomerizes via its C-terminal coiled-coil domain and, when overexpressed, inhibits RhoA-induced SRF activation without affecting RhoA-GTP levels. Mutant forms of p116Rip that fail to oligomerize or bind to MBS are still capable of inhibiting SRF activity. Our results suggest that p116Rip interferes with RhoA-mediated transcription through its ability to disassemble the actomyosin cytoskeleton downstream of RhoA. © 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Mulder, J., Ariaens, A., Van Horck, F. P. G., & Moolenaar, W. H. (2005). Inhibition of RhoA-mediated SRF activation by p116Rip. FEBS Letters, 579(27), 6121–6127. https://doi.org/10.1016/j.febslet.2005.09.083