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

Author: Zhang, X. F.; Settleman, J.; Kyriakis, J. M.; Takeuchi-Suzuki, E.; Elledge, S. J.; Marshall, M. S.; Bruder, J. T.; Rapp, U. R.; Avruch, J.

Description: 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.

Subject headings: Animals; Baculoviridae; Binding Sites; Cells; Cultured; Genetic Vectors; Moths; Mutation; Oncogene Protein p21(ras); Protein Binding; Protein Serine-Threonine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-raf; Proto-Oncogene Proteins p21(ras); Recombinant Fusion Proteins; Saccharomyces cerevisiae; Signal Transduction

Publication year: 1993

Journal or book title: Nature

Volume: 364

Issue: 6435

Pages: 308-313

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Serial number: 3926