Rho GTPase

spinqualitylabelsall models Human RhoA (magenta) complex with RhoGAP (cyan), GDP, AlF4 and Mg+2 ion (green) (PDB code 1tx4) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D 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. RhoB has a role in actin organisation, membrane trafficking, cell proliferation, DNA repair and apoptosis. RhoD participates in regulating cell-cycle progression and centrosome duplication. RhoE induces loss of stress fibres and inhibits cell cycle progression. RhoG regulates actin-cytoskeleton dynamics, survival and proliferation in immune cells. 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. Miro2 regulates inter-mitochondrial communication along microtubules. Disease Mutations in RhoA were identified in diffuse gastric cancer. Relevance RhoA is thought to be important in mediating vasoconstriction in the penis. Structural highlights The transition state complex of RhoA and RhoGAP contains GDP, AlF4 and Mg+2 ion. Water molecules are shown as red spheres. GDP binding site AlF4 and Mg+2 ion binding site. 3D structures of Rho GTPase Rho GTPase 3D structures

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