Prenylation of RhoB is required for its cell transforming function but not its ability to activate serum response element-dependent transcription

J Biol Chem. 1997 Jun 27;272(26):16093-5. doi: 10.1074/jbc.272.26.16093.

Abstract

Rho regulates cytoskeletal actin structure and integrin-mediated cell adhesion. Rho also has a role in cell growth regulation and is required for cell transformation by oncogenic Ras. Recently, it has been demonstrated that Rho can activate transcription from the c-fos serum response element (SRE). This raised the possibility that functions required for Rho-mediated cell transformation might overlap with those involved in transcriptional regulation. Here we show that RhoB can activate the SRE and can synergize in cell transformation with constitutively activated Raf-CAAX. Significantly, unprenylated forms of RhoB that are biologically inert and unable to transform cells can still activate SRE-dependent transcription. This finding suggests that transcriptional activation by Rho may be separable from its cell transforming functions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Animals
  • Cell Transformation, Neoplastic*
  • GTP-Binding Proteins / metabolism*
  • Genes, fos
  • Membrane Proteins / metabolism*
  • Mice
  • Protein Prenylation*
  • Transcription, Genetic*
  • rhoB GTP-Binding Protein

Substances

  • Membrane Proteins
  • GTP-Binding Proteins
  • rhoB GTP-Binding Protein