Rho2 palmitoylation is required for plasma membrane localization and proper signaling to the fission yeast cell integrity mitogen- activated protein kinase pathway.

ABSTRACT: The fission yeast small GTPase Rho2 regulates morphogenesis and is an upstream activator of the cell integrity pathway, whose key element, mitogen-activated protein kinase (MAPK) Pmk1, becomes activated by multiple environmental stimuli and controls several cellular functions. Here we demonstrate that farnesylated Rho2 becomes palmitoylated in vivo at cysteine-196 within its carboxyl end and that this modification allows its specific targeting to the plasma membrane. Unlike that of other palmitoylated and prenylated GTPases, the Rho2 control of morphogenesis and Pmk1 activity is strictly dependent upon plasma membrane localization and is not found in other cellular membranes. Indeed, artificial plasma membrane targeting bypassed the Rho2 need for palmitoylation in order to signal. Detailed

SUBMITTER: Sanchez-Mir L 

PROVIDER: S-EPMC4097651 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature