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Cell. 1991 Feb 8;64(3):511-20.

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

Author information

1
Department of Molecular and Cell Biology, University of California, Berkeley 94720.

Abstract

The T cell-specific transmembrane glycoprotein CD4 interacts with class II MHC molecules via its external domain and is associated with 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.

PMID:
1671341
DOI:
10.1016/0092-8674(91)90235-q
[Indexed for MEDLINE]

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