Oncogenic activation of human R-ras by point mutations analogous to those of prototype H-ras oncogenes

Oncogene. 1994 Oct;9(10):2977-82.

Abstract

R-ras, K-rev-1/rap and TC21, are more closely related to prototype H-ras than any other known members of the ras superfamily. We recently isolated a mutationally activated TC21 oncogene from a human ovarian carcinoma cell line. Based upon these observations, we sought to re-examine the transforming potential of R-ras, which was reported earlier to lack transforming capacity. Mutations were introduced into the R-ras gene at codons 38 or 87, analogous to positions 12 and 61, respectively, responsible for H-ras oncogene activation. While both mutations resulted in acquisition of R-ras transforming capacity for NIH3T3 cells the position 61 was shown to be more active. Transfectants expressing either R-ras mutant formed colonies in soft agar and were tumorigenic in vivo. As has been reported for H-ras, R-ras cooperated with c-raf-1 in inducing transformation of NIH3T3 cells. These results imply interactions in R-ras and c-raf-1 signaling pathways. We observed R-ras transcripts of 4.6 and 1.2 kb ubiquitously expressed in each of a variety of tissues examined. All these findings raise the possibility that R-ras, like prototype ras genes, may be mutationally activated as an oncogene in some human malignancies.

MeSH terms

  • 3T3 Cells
  • Animals
  • Base Sequence
  • Cell Transformation, Neoplastic / genetics*
  • DNA Primers
  • GTP Phosphohydrolases / genetics*
  • GTP-Binding Proteins / genetics*
  • Genes, ras*
  • Humans
  • Membrane Proteins / genetics
  • Mice
  • Molecular Sequence Data
  • Monomeric GTP-Binding Proteins*
  • Plasmids
  • Point Mutation*
  • Protein Serine-Threonine Kinases / genetics
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins c-raf
  • ras Proteins*

Substances

  • DNA Primers
  • Membrane Proteins
  • Proto-Oncogene Proteins
  • Protein Serine-Threonine Kinases
  • Proto-Oncogene Proteins c-raf
  • RRAS2 protein, human
  • Rras2 protein, mouse
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • RRAS protein, human
  • Rras protein, mouse
  • Monomeric GTP-Binding Proteins
  • ras Proteins