Requirement for association of p56lck with CD4 in antigen-specific signal transduction in T cells

Nicolas Glaichenhaus, Nilabh Shastri, Dan R. Littman, Julia M. Turner

Research output: Contribution to journalArticlepeer-review

341 Scopus citations

Abstract

The T cell-specific transmembrane glycoprotein CD4 interacts with class 11 MHC molecules via its external domain and is associated with the tyrosine kinase p56lck via a cysteine motif in its cytoplasmic domain. We have assessed the ability of CD4 to synergize with the antigen-specific T cell receptor (TCR) for induction of transmembrane signals that result in lymphokine production. Mutant CD4 molecules were introduced into T cells that lacked endogenous CD4 but expressed TCRs specific for lysozyme peptides or the superantigen SEA bound to Ab or Abm12 class II MHC molecules. With either ligand, T cell activation occurred only when CD4 was associated with p56lck. These results demonstrate that residues within the cytoplasmic domain of CD4 are required for its coreceptor function in TCR-mediated signal transduction and strongly support the notion that the association of CD4 with p56lck is critical in this process.

Original languageEnglish (US)
Pages (from-to)511-520
Number of pages10
JournalCell
Volume64
Issue number3
DOIs
StatePublished - Feb 8 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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