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Vol. 9, Issue 2, 451-467, February 1998
*
*Molecular Mechanisms of Growth Control Group, Department of Cell
Biology and Anatomy, University of Alberta, Edmonton, Alberta T6G 2H7,
and
We have added constitutively active MAP kinase/ERK kinase (MEK), an
activator of the mitogen-activated protein kinase (MAPK) signaling
pathway, to cycling Xenopus egg extracts at various times during the cell cycle. p42MAPK activation during entry into M-phase arrested the cell cycle in metaphase, as has been shown previously. Unexpectedly, p42MAPK activation during interphase inhibited entry into M-phase. In these interphase-arrested extracts, H1
kinase activity remained low, Cdc2 was tyrosine phosphorylated, and
nuclei continued to enlarge. The interphase arrest was overcome by
recombinant cyclin B. In other experiments, p42MAPK activation by MEK
or by Mos inhibited Cdc2 activation by cyclin B. PD098059, a specific
inhibitor of MEK, blocked the effects of MEK(QP) and Mos. Mos-induced
activation of p42MAPK did not inhibit DNA replication. These results
indicate that, in addition to the established role of p42MAPK
activation in M-phase arrest, the inappropriate activation of p42MAPK
during interphase prevents normal entry into M-phase.
Department of Biological Sciences, University of
Calgary, Calgary, Alberta T2N 1N4, Canada
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