Signal transduction through the CD4 receptor involves the activation of the internal membrane tyrosine-protein kinase p56lck
摘要：
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 activation 2–4 . It has recently been shown that CD4 expressed on human 5,6 and murine 6 T cells is physically associated with the Src-related tyrosine protein kinase p56 lck (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 p56 lck 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 p56 lck and suggest that some of the tyrosine phosphorylation events detected during antigen-mediated T-cell activation may result from signalling through this surface molecule.
展开
DOI：
10.1038/338257a0
被引量：
年份：
1989
相似文献
参考文献
引证文献
辅助模式
引用
文献可以批量引用啦~
欢迎点我试用！
