A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction

Harry M. Lander, David P. Hajjar, Barbara L. Hempstead, Urooj A. Mirza, Brian T. Chait, Sharon Campbell, Lawrence A. Quilliam

Research output: Contribution to journalArticle

430 Scopus citations

Abstract

We have identified the site of molecular interaction between nitric oxide (NO) and p21(ras) responsible for initiation of signal transduction. We found that p21(ras) was singly S-nitrosylated and localized this modification to a fragment of p21(ras) containing Cys118. A mutant form of p21(ras), in which Cys118 was changed to a serine residue and termed p21(ras)C118S, was not S-nitrosylated. NO-related species stimulated guanine nucleotide exchange on wild-type p21(ras), resulting in an active form, but not on p2(ras)C118S. Furthermore, in contrast to parental Jurkat T cells, NO-related species did not stimulate mitogen-activated protein kinase activity in cells transfected with p21(ras)C118S. These data indicate that Cys118 is a critical site of redox regulation of p21(ras), and S-nitrosylation of this residue triggers guanine nucleotide exchange and downstream signaling.

Original languageEnglish (US)
Pages (from-to)4323-4326
Number of pages4
JournalJournal of Biological Chemistry
Volume272
Issue number7
DOIs
StatePublished - Feb 25 1997

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'A molecular redox switch on p21(ras). Structural basis for the nitric oxide-p21(ras) interaction'. Together they form a unique fingerprint.

  • Cite this