Interleukin-2-induced tyrosine phosphorylation of p52shc in T lymphocytes

Leigh Ann Burns, Larry M. Karnitz, Shari L. Sutor, Robert T. Abraham

Research output: Contribution to journalArticlepeer-review

73 Scopus citations


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, p52shc, on both tyrosine and serine residues. The level of p52shc 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 p52shc on tyrosine residues in immune complex kinase assays. These results demonstrate that p52shc 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
Issue number24
StatePublished - Aug 25 1993

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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