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Complex formation between RAS and RAF and other protein kinases.

We used a Saccharomyces cerevisiae genetic system to detect the physical interaction of RAS and RAF oncoproteins. We also observed interaction between RAS and byr2, a protein kinase implicated as a mediator of the Schizosaccharomyces pombe ras1 protein. Interaction with RAS required only the N-terminal domains of RAF or byr2 and was disrupted by mutations in either the guanine nucleotide-binding or effector-loop domains of RAS. We observed interaction between MEK (a kinase that phosphorylates mitogen-activated protein kinases) and the catalytic domain of RAF. RAS and MEK also interacted but only when RAF was overexpressed.

Pubmed ID: 8327501


  • Van Aelst L
  • Barr M
  • Marcus S
  • Polverino A
  • Wigler M


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

Publication Data

July 1, 1993

Associated Grants


Mesh Terms

  • Base Sequence
  • Fungal Proteins
  • GTP-Binding Proteins
  • Guanosine Triphosphate
  • MAP Kinase Kinase 1
  • Mitogen-Activated Protein Kinase Kinases
  • Molecular Sequence Data
  • Protein Kinases
  • Protein-Serine-Threonine Kinases
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Proto-Oncogene Proteins c-raf
  • Proto-Oncogene Proteins p21(ras)
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins
  • ras Proteins