Dimerization of Ste5, a mitogen-activated protein kinase cascade scaffold protein, is required for signal transduction

• DOI: 10.1073/pnas.93.24.13864
• Publication Date: 2002-07-26T14:35:50Z
• Authors: Deborah Yablonski; Irit Marbach; Alexander Levitzki
• Keywords: Immunoprecipitation; Protein-fragment complementation assay

The mitogen-activated protein kinase cascade of the Saccharomyces cerevisiae pheromone response pathway is organized on Ste5 protein, which binds each kinases prior to signaling. In this study, a structure–function analysis deletion mutants uncovered new functional domains and revealed that dimerizes during course normal signal transduction. Dimerization, mediated by two regions in N-terminal half Ste5, was first suggested intragenic complementation between pairs nonfunctional confirmed using two-hybrid system. Coimmunoprecipitation differently tagged forms from cells has been activated overexpression further dimerization. A precise correlation biological activity various fragments dimerization suggests essential for function.