A role for the Ral guanine nucleotide dissociation stimulator in mediating Ras-induced transformation

Michael A. White, Terry Vale, Jacques H. Camonis, Erik Schaefer, Michael H. Wigler

Research output: Contribution to journalArticle

210 Scopus citations

Abstract

Oncogenic Ras transforms cells through the activation of multiple downstream pathways mediated by separate effector molecules, one of which is Raf. Here we report the identification era second ras-binding protein that can induce cellular transformation in parallel with activation of the Raf/mitogen-activated protein kinase cascade. The Ral guanine nucleotide dissociation stimulator (RalGDS) was isolated from a screen for Ras-binding proteins that specifically interact with a Ras effector-loop mutant, ras(12V,37G), that uncouples Ras from activation of Raf1. RalGDS, like ras(12V,37G), cooperates synergistically with mutationally activated Raf to induce foci of growth and morphologically transformed NIH 3T3 cells. RalGDS does not significantly enhance MAP kinase activation by activated Raf, suggesting that the cooperativity in focus formation is due to a distinct pathway acting downstream of Ras and parallel to Raf.

Original languageEnglish (US)
Pages (from-to)16439-16442
Number of pages4
JournalJournal of Biological Chemistry
Volume271
Issue number28
DOIs
StatePublished - Jul 30 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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