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Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator.

The yeast two-hybrid system was used to identify proteins that interact with Ras. The H-Ras protein was found to interact with a guanine nucleotide dissociation stimulator (GDS) that has been previously shown to regulate guanine nucleotide exchange on another member of the Ras protein family, Ral. The interaction is mediated by the C-terminal, noncatalytic segment of the RalGDS and can be detected both in vivo, using the two-hybrid system, and in vitro, with purified recombinant proteins. The interaction of the RalGDS C-terminal segment with Ras is specific, dependent on activation of Ras by GTP, and blocked by a mutation that affects Ras effector function. These characteristics are similar to those previously demonstrated for the interaction between Ras and its putative effector, Raf, suggesting that the RalGDS may also be a Ras effector. Consistent with this idea, the RalGDS was found to inhibit the binding of Raf to Ras.

Pubmed ID: 7972015

Authors

  • Hofer F
  • Fields S
  • Schneider C
  • Martin GS

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Data

November 8, 1994

Associated Grants

  • Agency: NCI NIH HHS, Id: CA17542
  • Agency: NCI NIH HHS, Id: CA28146

Mesh Terms

  • Amino Acid Sequence
  • Binding Sites
  • Binding, Competitive
  • GTP-Binding Proteins
  • Humans
  • In Vitro Techniques
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • Protein Binding
  • Protein-Serine-Threonine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-raf
  • Proto-Oncogene Proteins p21(ras)
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • ral GTP-Binding Proteins