Abstract
Rho GTPases
Highlights
Rho proteins control the organization of the actin cytoskeleton in all eukaryotic cells
The exact role of the Rho GTPases in MAP kinase activation is, far from clear; overexpression of constitutively activated Rac or Cdc42 leads to only modest activation of JNK reporter plasmids in cotransfection assays, and there are still very few examples where physiological activation of the JNK pathway has been shown to be dependent on endogenous Rac or Cdc42 activity
Rac, and Cdc42 activities are required during G1 cell cycle progression, but whether this is because of their effects on the actin cytoskeleton and integrin adhesion complexes or whether it is because of more direct effects on gene transcription is not known (16 –20)
Summary
From the ‡Medical Research Council Laboratory for Molecular Cell Biology, §Cancer Research Campaign Oncogene and Signal Transduction Group, and §Department of Biochemistry, University College London, Gower Street, London, WC1E 6BT, United Kingdom. The mammalian Rho GTPase family currently consists of seven distinct proteins: Rho (A, B, and C isoforms), Rac (1 and 2 isoforms), Cdc (Cdc42Hs and G25K isoforms), RhoD, RhoG, RhoE, and TC10. Like other members of the Ras superfamily, Rho proteins act as molecular switches to control cellular processes by cycling between active, GTP-bound and inactive, GDPbound states (Fig. 1). Rho guanine nucleotide dissociation inhibitors (Rho-GDIs) appear to stabilize the inactive, GDP-bound form of the protein. Activated Rho GTPases interact with cellular target proteins or effectors to trigger a wide variety of cellular responses, including the reorganization of the actin cytoskeleton and changes in gene transcription. This review aims to summarize current views of Rho GTPase signaling pathways; for reasons of space, this will be limited primarily to mammalian Rho, Rac, and Cdc. More detailed information can be found elsewhere [1, 2]
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