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Science 14 February 1992:
Vol. 255. no. 5046, pp. 853 - 855
DOI: 10.1126/science.1311128
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Articles

Science, Vol 255, Issue 5046, 853-855
Copyright © 1992 by American Association for the Advancement of Science

articles

Tyrosyl phosphorylation and activation of MAP kinases by p56lck

E Ettehadieh, JS Sanghera, SL Pelech, D Hess-Bienz, J Watts, N Shastri, and R Aebersold

Biomedical Research Centre, University of British Columbia, Vancouver, Canada.

T cell signaling via the CD4 surface antigen is mediated by the associated tyrosyl protein kinase p56lck. The 42-kilodalton mitogen-activated protein (MAP) kinase (p42mapk) was tyrosyl-phosphorylated and activated after treatment of the murine T lymphoma cell line 171CD4+, which expresses CD4, with antibody to CD3. Treatment of the CD4-deficient cell line 171 with the same antibody did not result in phosphorylation or activation of p42mapk. Purified p56lck both tyrosyl-phosphorylated and stimulated the seryl-threonyl phosphotransferase activity of purified p44mpk, a MAP kinase isoform from sea star oocytes. A synthetic peptide modeled after the putative regulatory phosphorylation site in murine p42mapk (Tyr185) was phosphorylated by p56lck with a similar Vmax, but a fivefold lower Michaelis constant (Km) than a peptide containing the Tyr394 autophosphorylation site from p56lck. MAP kinases may participate in protein kinase cascades that link Src family protein-tyrosyl kinases to seryl-threonyl kinases such as those encoded by rsk and raf, which are putative substrates of MAP kinases.


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