RICH-1, a multifunctional RhoGAP domain-containing protein, involved in regulation of the actin filament system and membrane-trafficking.

摘要: A previously unidentified Rho GTPase-activating protein (GAP) domain-containing was found in a yeast two-hybrid screen for cDNAs encoding proteins binding to the Src homology 3 domain of Cdc42-interacting 4 (CIP4). The named RICH-1 (RhoGAP interacting with CIP4 homologues), and, addition RhoGAP domain, it contained an N-terminal endophilin and C-terminal proline-rich domain. Transient transfections indicated that bound vivo, as shown by co-immunoprecipitation experiments, well co-localization assays. In vitro assays demonstrated catalyzed GTP hydrolysis on Cdc42 Rac1, but not RhoA. Ectopic expression full-length interfered platelet-derived growth factor BB-induced membrane ruffling, serum-induced stress fiber formation, further emphasizing notion that, is GAP Rac1.