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Mol. Cell. Biol., 03 1996, 1247-1255, Vol 16, No. 3
J Raingeaud, AJ Whitmarsh, T Barrett, B Derijard and RJ Davis
The p38 mitogen-activated protein (MAP) kinase signal transduction pathway
is activated by proinflammatory cytokines and environmental stress. The
detection of p38 MAP kinase in the nucleus of activated cells suggests that
p38 MAP kinase can mediate signaling to the nucleus. To test this
hypothesis, we constructed expression vectors for activated MKK3 and MKK6,
two MAP kinase kinases that phosphorylate and activate p38 MAP kinase.
Expression of activated MKK3 and MKK6 in cultured cells caused a selective
increase in p38 MAP kinase activity. Cotransfection experiments
demonstrated that p38 MAP kinase activation causes increased reporter gene
expression mediated by the transcription factors ATF2 and Elk-1. These data
demonstrate that the nucleus is one target of the p38 MAP kinase signal
transduction pathway.
Copyright © 1996, American Society for Microbiology
MKK3- and MKK6-regulated gene expression is mediated by the p38 mitogen- activated protein kinase signal transduction pathway
Howard Hughes Medical Institute and Program in Molecular Medicine, University of Massachusetts Medical School, Worcester 01605 USA.
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