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Science 28 July 1989:
Vol. 245. no. 4916, pp. 407 - 409
DOI: 10.1126/science.2787934
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Articles

Science, Vol 245, Issue 4916, 407-409
Copyright © 1989 by American Association for the Advancement of Science

articles

Activators of protein kinase C induce dissociation of CD4, but not CD8, from p56lck

TR Hurley, K Luo, and BM Sefton

Molecular Biology and Virology Laboratory, Salk Institute, San Diego, CA 92138.

The CD4 and CD8 T cell receptor accessory molecules can both be isolated from T lymphocytes in association with p56lck, a membrane-associated, cytoplasmic tyrosine protein kinase that is expressed exclusively in lymphoid cells. The enzymatic activity of p56lck 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 p56lck and CD4. Activation of protein kinase C may therefore interrupt regulation of p56lck by CD4 and alter the ability of p56lck to interact with polypeptide substrates. In contrast, exposure of cells to TPA did not cause dissociation of p56lck and CD8. Regulation of p56lck by CD4 may therefore differ from regulation by CD8.


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