Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p56lck View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1989-03

AUTHORS

André Veillette, Michael A. Bookman, Eva M. Horak, Lawrence E. Samelson, Joseph B. Bolen

ABSTRACT

THE CD4 T-cell surface antigen is an integral membrane gly-coprotein of relative molecular mass 55,000 which binds class II major histocompatibility complex (MHC) molecules expressed on antigen presenting cells (APCs). It is thought to stabilize physical interactions between T cells and APCs (for a review, see ref. 1). Evidence is accumulating that suggests that CD4 can transduce an independent signal during T-cell activation2–4. It has recently been shown that CD4 expressed on human5,6 and murine6 T cells is physically associated with the Src-related tyrosine protein kinase p56lck (refs 7, 8). These results indicate that CD4 can function as a signal transducer and suggest that tyrosine phosphorylation events may be important in CD4-mediated signalling. Here, we present evidence that cross-linking of the CD4 receptor induces a rapid increase in the tyrosine-specific protein kinase activity of p56lck and is associated with the rapid phosphorylation of one of the subunits (ζ) of the T-cell receptor complex on tyrosine residues. These data provide direct evidence for a specific CD4 signal transduction pathway that is mediated through p56lck and suggest that some of the tyrosine phosphorylation events detected during antigen-mediated T-cell activation may result from signalling through this surface molecule. More... »

PAGES

257-259

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/338257a0

DOI

http://dx.doi.org/10.1038/338257a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1034083801

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2784195


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