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
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Baculoviridae / genetics
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Binding Sites
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Cells, Cultured
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Genetic Vectors
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Moths
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Mutation
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Oncogene Protein p21(ras) / metabolism*
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Protein Binding
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Protein Serine-Threonine Kinases / metabolism*
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-raf
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Proto-Oncogene Proteins p21(ras) / metabolism*
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Recombinant Fusion Proteins / metabolism
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Saccharomyces cerevisiae
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Signal Transduction / physiology
Substances
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Proto-Oncogene Proteins
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Recombinant Fusion Proteins
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Protein Serine-Threonine Kinases
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Proto-Oncogene Proteins c-raf
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Oncogene Protein p21(ras)
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Proto-Oncogene Proteins p21(ras)