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J. Biol. Chem., Vol. 266, Issue 7, 4220-4227, Mar, 1991
NG Ahn, R Seger, RL Bratlien, CD Diltz, NK Tonks and EG Krebs
Epidermal growth factor stimulates the activity of several cytosolic
serine/threonine protein kinases in quiescent Swiss 3T3 cells. Two of
these, which use myelin basic protein (MBP) as substrate, act as kinase
kinases in that they are able to activate a separate peptide kinase
activity in vitro by a mechanism involving protein phosphorylation. In this
study, we have identified two activities from extracts of epidermal growth
factor-treated cells that stimulate an ATP-dependent activation of both of
the MBP kinases, derived in their inactive precursor forms from extracts of
untreated cells. The resulting MBP kinase activities are stable to further
purification and can be inactivated with either tyrosine or
serine/threonine protein phosphatases and then reactivated to their
original levels of activity. Thus, we propose that the in vitro activation
involves protein phosphorylation, stimulated by the action of novel MBP
kinase activating factors that represent intermediate components in a
growth factor-stimulated kinase cascade.
Multiple components in an epidermal growth factor-stimulated protein kinase cascade. In vitro activation of a myelin basic protein/microtubule-associated protein 2 kinase
Department of Biochemistry, University of Washington, Seattle 98195.
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