Lck regulates the tyrosine phosphorylation of the T cell receptor subunits and ZAP-70 in murine thymocytes

Nicolai S C Van Oers, Nigel Killeen, Arthur Weiss

Research output: Contribution to journalArticle

266 Scopus citations

Abstract

The Src-family and Syk/ZAP-70 family of protein tyrosine kinases (PTK) are required for T cell receptor (TCR) functions. We provide evidence that the Src-family PTK Lck is responsible for regulating the constitutive tyrosine phosphorylation of the TCR ζ subunit in murine thymocytes. Moreover, ligation of the TCR expressed on thymocytes from Lck-deficient mice largely failed to induce the phosphorylation of TCR-ζ, CD3ε, or ZAP-70. In contrast, we find that the TCR-ζ subunit is weakly constitutively tyrosine phosphorylated in peripheral T cells isolated from Lck-null mice. These data suggest that Lck has a functional role in regulation of TCR signal transduction in thymocytes. In peripheral T cells, other Src-family PTKs such as Fyn may partially compensate for the absence of Lck.

Original languageEnglish (US)
Pages (from-to)1053-1062
Number of pages10
JournalJournal of Experimental Medicine
Volume183
Issue number3
DOIs
StatePublished - Mar 1 1996

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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