Evidence for a high affinity, saturable, prenylation-dependent p21Ha-ras binding site in plasma membranes

J Biol Chem. 1998 Feb 6;273(6):3712-7. doi: 10.1074/jbc.273.6.3712.

Abstract

Oncogenic p21ras proteins can only exert their stimulation of cellular proliferation when plasma membrane-associated. This membrane association has an absolute requirement for post-translational modification with isoprenoids. The mechanism by which isoprenoids participate in the specific association of p21ras with plasma membranes is the subject of this report. We present in vitro evidence for a plasma membrane binding protein for p21(ras) that can recognize the isoprenoid substituent and, therefore, may facilitate the localization of p21ras.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Cell Membrane / metabolism
  • Ligands
  • Mice
  • Molecular Sequence Data
  • Protein Prenylation
  • Proto-Oncogene Proteins p21(ras) / metabolism*

Substances

  • Ligands
  • Proto-Oncogene Proteins p21(ras)