RhoA regulates a signal transduction pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. It is involved in a microtubule-dependent signal that is required for the myosin contractile ring formation during cell cycle cytokinesis, and plays an essential role in cleavage furrow formation. RhoA is required for the apical junction formation of keratinocyte cell-cell adhesion, and serves as a target for the yopT cysteine peptidase from Yersinia pestis, vector of the plague, and Yersinia pseudotuberculosis, which causes gastrointestinal disorders. RhoA stimulates PKN2 kinase activity and may be an activator of PLCE1. It is activated by ARHGEF2, which promotes the exchange of GDP for GTP. It is essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization.
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Protein Aliases: Aplysia ras-related homolog 12; h12; MGC72339; oncogene RHO H12; Rho; Rho cDNA clone 12; small GTP binding protein RhoA; Transforming protein RhoA
Gene Aliases: ARH12; ARHA; RHO12; RHOA; RHOH12
UniProt ID: (Human) P61586
Entrez Gene ID: (Human) 387
Molecular Function: small GTPase