CaM interaction and Ser181 phosphorylation as new K-Ras signaling modulators

• DOI: 10.4161/sgtp.2.2.15555
• Publication Date: 2011-04-28T18:23:20Z
• Authors: Blanca Alvarez-Moya; Carles Barceló; Francesc Tebar; Montserrat Jaumot; Neus Agell
• Keywords: Small GTPase; HEK 293 cells

The small G-protein Ras was the first oncogene to be identified and has a very important contribution human cancer development (20-23% prevalence). K-RasB, one of members family, is that most mutated plays prominent role in pancreatic, colon lung development. proteins are membrane bound GTPases cycle between inactive, GDP-bound active, GTP-bound, states. Most research into K-RasB activity regulation focused on analysis how GTP-exchange factors (GEFs) GTPase activating (GAPs) regulated by external internal signals. In contrast, oncogenic low furthermore not deactivated GAPs. Consequently, consensus modulated. this extra view we recapitulate some recent data showing calmodulin binding inhibits phosphorylation at Ser181, near anchoring domain, modulating signaling both non-oncogenic K-RasB. This may relevant normal cell physiology, but also opens new therapeutic perspectives for inhibition tumors.