Oligomerization-dependent and synergistic regulation of Cdc42 GTPase cycling by a GEF and a GAP

ABSTRACT: Cell polarity is a crucial biological process essential for cell division, directed growth, and motility. In Saccharomyces cerevisiae, polarity establishment centers around the small Rho-type GTPase Cdc42, which cycles between GTP-bound and GDP-bound states, regulated by GEFs like Cdc24 and GAPs such as Rga2. To dissect the dynamic regulation of Cdc42, we employed in vitro GTPase assays, revealing inverse concentration-dependent profiles for Cdc24 and Rga2: with increasing concentration, Cdc24's GEF activity is non-linear and oligomerization-dependent, which is possibly linked to the relief of its self-inhibition. In contrast, Rga2's GAP activity saturates, likely due to self-inhibition upon oligomerization. Together, Cdc24 and Rga2 exhibit a strong synergy driven by weak Cdc24 - Rga2 bindi

SUBMITTER: Sophie Tschirpke 

PROVIDER: S-SCDT-10_1038-S44319-026-00695-7 | biostudies-other |

REPOSITORIES: biostudies-other