A nuclear MAL-function links Rho to SRF

Mol Cell. 2003 May;11(5):1121-3. doi: 10.1016/s1097-2765(03)00189-8.

Abstract

The activation of SRF-mediated transcription in response to Rho GTPase-induced actin assembly involves the ability of SRF to sense changes in the cellular level of actin monomers. An article in the May 2 issue of Cell identifies the transcription factor MAL as an actin binding protein that functions as an SRF coactivator and whose translocation from cytoplasm to nucleus depends on its dissociation from actin monomers (Miralles et al., 2003).

Publication types

  • Review

MeSH terms

  • Actins / biosynthesis*
  • Active Transport, Cell Nucleus / genetics
  • Animals
  • Cell Nucleus / metabolism*
  • Cell Nucleus / ultrastructure
  • Eukaryotic Cells / cytology
  • Eukaryotic Cells / metabolism*
  • Gene Expression Regulation / genetics
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • MAP Kinase Kinase Kinases / genetics
  • MAP Kinase Kinase Kinases / metabolism*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Serum Response Factor / genetics
  • Serum Response Factor / metabolism*
  • rho GTP-Binding Proteins / genetics
  • rho GTP-Binding Proteins / metabolism*
  • rho-Associated Kinases

Substances

  • Actins
  • Intracellular Signaling Peptides and Proteins
  • Serum Response Factor
  • Protein Serine-Threonine Kinases
  • rho-Associated Kinases
  • MAP Kinase Kinase Kinases
  • MAP3K9 protein, human
  • rho GTP-Binding Proteins