Function
Rho GTPase or Rho-related GTP-binding protein of higher vertebrates include RhoA, RhoB, RhoC, RhoD and RhoE. These proteins share 85% sequence identity. RhoA is the more extensively studied among these three. RhoA regulates a signal transduction phosphorylation pathway linking plasma membrane receptors to the assembly of focal adhesions and actin stress fibers. Rho GTPase operates as a switch cycling between the active GTP-bound form and the inactive GDP-bound one. A number of proteins have been identified as targets of RhoA[1]. Mitochondrial Rho GTPase (Miro) have tandem GTP-binding domains separated by a linker region containing calcium-binding EF hand motifs indicating a role in mitochondrial homeostasis and apoptosis[2].
Disease
Mutations in RhoA were identified in diffuse gastric cancer[3].
Relevance
RhoA is thought to be important in mediating vasoconstriction in the penis[4].
Structural highlights
The [5]. Water molecules are shown as red spheres.
3D structures of Rho GTPase
Rho GTPase 3D structures
