Rewiring MAP kinases in Saccharomyces cerevisiae to regulate novel targets through ubiquitination.

ABSTRACT: Evolution has often copied and repurposed the mitogen-activated protein kinase (MAPK) signaling module. Understanding how connections form during evolution, in disease and across individuals requires knowledge of the basic tenets that govern kinase-substrate interactions. We identify criteria sufficient for establishing regulatory links between a MAPK and a non-native substrate. The yeast MAPK Fus3 and human MAPK ERK2 can be functionally redirected if only two conditions are met: the kinase and substrate contain matching interaction domains and the substrate includes a phospho-motif that can be phosphorylated by the kinase and recruit a downstream effector. We used a panel of interaction domains and phosphorylation-activated degradation motifs to demonstrate modular and scalable retargetin

SUBMITTER: Groves B 

PROVIDER: S-EPMC5019841 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature