Activators of Protein Kinase C Induce Dissociation of CD4, but not CD8, from p56$^{lck}

The CD4 and CD8 T cell receptor accessory molecules can both be isolated from T lymphocytes in association with p56$^{lck}$, a membrane-associated, cytoplasmic tyrosine protein kinase that is expressed exclusively in lymphoid cells. The enzymatic activity of p56$^{lck}$ may therefore be regulated by...

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Bibliographic Details
Published inScience (American Association for the Advancement of Science) Vol. 245; no. 4916; pp. 407 - 409
Main Authors Hurley, Tamara R., Luo, Kunxin, Sefton, Bartholomew M.
Format Journal Article
LanguageEnglish
Published The American Association for the Advancement of Science 28.07.1989
Subjects
Antibodies
Cell lines
Gels
Internalization
Lymphocytes
Mice
Phosphorylation
Physiological regulation
T lymphocytes
Thymocytes
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Summary:The CD4 and CD8 T cell receptor accessory molecules can both be isolated from T lymphocytes in association with p56$^{lck}$, a membrane-associated, cytoplasmic tyrosine protein kinase that is expressed exclusively in lymphoid cells. The enzymatic activity of p56$^{lck}$ may therefore be regulated by CD4 and CD8 and be important in antigen-induced T cell activation. Exposure of human T cells and some mouse T cells to the tumor promoter 12-O-tetradecanoyl phorbol-13-acetate (TPA), an activator of protein kinase C, caused the dissociation of p56$^{lck}$ and CD4. Activation of protein kinase C may therefore interrupt regulation of p56$^{lck}$ by CD4 and alter the ability of p56$^{lck}$ to interact with polypeptide substrates. In contrast, exposure of cells to TPA did not cause dissociation of p56$^{lck}$ and CD8. Regulation of p56$^{lck}$ by CD4 may therefore differ from regulation by CD8.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2787934