Interleukin-2-induced tyrosine phosphorylation of p52(shc) in T lymphocytes

L. A. Burns, L. M. Karnitz, S. L. Sutor, R. T. Abraham

Research output: Contribution to journalArticle

72 Scopus citations

Abstract

Stimulation of activated T cells with interleukin-2 (IL-2) results in the tyrosine phosphorylation of several intracellular proteins. The present studies demonstrate that IL-2 stimulation induces phosphorylation of the src homology 2 domain-containing protein, p52(shc), on both tyrosine and serine residues. The level of p52(shc) phosphorylation was maximal within 5 min after growth factor addition and declined gradually thereafter. In addition, anti-Shc immunoprecipitates from IL-2-stimulated T cells contained a co- precipitating protein tyrosine kinase (PTK) activity that phosphorylated p52(shc) on tyrosine residues in immune complex kinase assays. These results demonstrate that p52(shc) is an early substrate for IL-2 receptor-coupled PTK activity(s) and suggest that this protein may be involved in the transduction of PTK-dependent regulatory signals in IL-2-stimulated T cells.

Original languageEnglish (US)
Pages (from-to)17659-17661
Number of pages3
JournalJournal of Biological Chemistry
Volume268
Issue number24
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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