Linking TGF-beta-mediated Cdc25A inhibition and cytoskeletal regulation through RhoA/p160(ROCK) signaling

Cell Cycle. 2004 Apr;3(4):408-10. Epub 2004 Apr 1.

Abstract

Transforming growth factor-beta (TGF-beta) can mediate G(1)/S cell-cycle inhibition and changes in the cytoskeletal organization through multiple parallel downstream signaling pathways. Recent findings regarding TGF-beta-mediated cell-cycle checkpoint control and epithelial to mesenchymal transition have converged to the RhoA/p160(ROCK) signaling pathway. The activation of TGF-beta-mediated p160(ROCK)rapidly inhibits the Cdc25A phosphatase as a component of the G(1)/S checkpoint control at the time cytoskeletal re-organization occurs. This can be likened to the ability to preserve genomic integrity in circumstances of genotoxic stress. The inactivation of the RhoA/p160(ROCK) pathway may be a mechanism by which cancer cells bypass growth inhibition even in the presence of TGF-beta.

MeSH terms

  • Animals
  • Cell Cycle
  • Cell Division
  • Cytoskeleton / metabolism*
  • Disease Progression
  • G1 Phase
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Mice
  • NIH 3T3 Cells
  • Neoplasms / metabolism
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • S Phase
  • Signal Transduction*
  • Transforming Growth Factor beta / metabolism*
  • cdc25 Phosphatases / metabolism*
  • rho-Associated Kinases
  • rhoA GTP-Binding Protein / metabolism*

Substances

  • Intracellular Signaling Peptides and Proteins
  • Transforming Growth Factor beta
  • Protein Serine-Threonine Kinases
  • rho-Associated Kinases
  • CDC25A protein, human
  • Cdc25a protein, mouse
  • cdc25 Phosphatases
  • rhoA GTP-Binding Protein