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J. Biol. Chem., Vol. 276, Issue 10, 6905-6908, March 9, 2001
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From the We have identified a direct physical interaction
between the stress signaling p38 Department of Medicine, Koerner
Pavilion, University of British Columbia, Vancouver, British Columbia
V6T 1Z3 and the § Kinexus Bioinformatics Corporation,
Vancouver, British Columbia V6T 1Z4, Canada
MAP kinase and the
mitogen-activated protein kinases ERK1 and ERK2 by affinity
chromatography and coimmunoprecipitation studies. Phosphorylation and
activation of p38 enhanced its interaction with ERK1/2, and this
correlated with inhibition of ERK1/2 phosphotransferase activity. The
loss of epidermal growth factor-induced activation and
phosphorylation of ERK1/2 but not of their direct activator MEK1 in
HeLa cells transfected with the p38 activator MKK6(E) indicated that
activated p38 may sequester ERK1/2 and sterically block their
phosphorylation by MEK1.
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