The biochemical mechanism of Rho GTPase membrane binding, activation and retention in activity patterning

ABSTRACT: Rho GTPases form plasma membrane-associated patterns that control the cytoskeleton during cell division, morphogenesis, migration, and wound repair. Their patterning involves transitions between inactive cytosolic and active membrane-bound states, regulated by guanine nucleotide exchange factors (GEFs), GTPase-activating proteins (GAPs), and guanine nucleotide dissociation inhibitors (GDIs). However, the relationships between these transitions and role of different regulators remain unclear. We developed a novel reconstitution approach to study Rho GTPase patterning with all major GTPase regulators in a biochemically defined system. We show that Rho GTPase dissociation from RhoGDI is rate-limiting for its membrane association. Rho GTPase activation occurs after membrane insertion, which is

SUBMITTER: Michael, C Armstrong 

PROVIDER: S-SCDT-10_1038-S44318-025-00418-Z | biostudies-other |

REPOSITORIES: biostudies-other