Normal and oncogenic p21ras proteins bind to the amino-terminal regulatory domain of c-Raf-1

Nature. 1993 Jul 22;364(6435):308-13. doi: 10.1038/364308a0.

Abstract

In higher eukaryotes, the Ras and Raf-1 proto-oncoproteins transduce growth and differentiation signals initiated by tyrosine kinases. The Ras polypeptide and the amino-terminal regulatory domain of Raf-1 (residues 1-257) are shown to interact, directly in vitro and in a yeast expression system. Raf-1 (1-257) binds GTP-Ras in preference to GDP-Ras, and inhibits Ras-GAP activity. Mutations in and around the Ras effector domain impair Ras binding to Raf-1 (1-257) and Ras transforming activity in parallel.

Publication types

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

MeSH terms

  • Animals
  • Baculoviridae / genetics
  • Binding Sites
  • Cells, Cultured
  • Genetic Vectors
  • Moths
  • Mutation
  • Oncogene Protein p21(ras) / metabolism*
  • Protein Binding
  • Protein-Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins c-raf
  • Proto-Oncogene Proteins p21(ras) / metabolism*
  • Recombinant Fusion Proteins / metabolism
  • Saccharomyces cerevisiae
  • Signal Transduction / physiology

Substances

  • Proto-Oncogene Proteins
  • Recombinant Fusion Proteins
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-raf
  • Oncogene Protein p21(ras)
  • Proto-Oncogene Proteins p21(ras)