RhoV

RhoV is a member of the Rho family of small GTPases, a group of enzymes that act as molecular switches in the cell. It cycles between an active GTP-bound state and an inactive GDP-bound state, a process regulated by guanine nucleotide exchange factors (GEFs), GTPase-activating proteins (GAPs), and guanine nucleotide dissociation inhibitors (GDIs). In humans it is commonly referred to as RhoV and is sometimes called Chp in the literature.

The protein contains the characteristic GTPase domain and is typically modified at its C-terminus to promote membrane association, such as prenylation of a CaaX-like motif. This lipid modification helps localize RhoV to the plasma membrane and intracellular membranes where it can participate in signaling events that control the actin cytoskeleton.

Functionally, RhoV is implicated in the regulation of actin dynamics, cell shape, and cell–cell junctions. Its activity influences cortical actin remodeling and can affect cell migration and adhesion in a context-dependent manner. Downstream signaling often involves actin-regulatory pathways and may include interactions with WASP-family proteins and other effectors that shape the cytoskeleton; exact pathways can vary by cell type and stimulus.

Expression patterns show notable activity in vascular and neural tissues, particularly during development, though detailed tissue-specific roles are still under investigation. In developmental and cancer biology, alterations in RhoV signaling have been linked to processes such as vascular morphogenesis and endothelial barrier function, but many aspects of its physiological roles remain to be fully defined.

Overall, RhoV is a relatively less-studied member of the Rho GTPase family, and ongoing research aims to clarify its regulatory partners, cellular contexts, and contributions to physiology and disease.