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Vol. 8, Issue 11, 2157-2169, November 1997
Department of Molecular Pharmacology, Stanford University School of
Medicine, Stanford, California 94305-5332
Previous work has established that activation of Mos, Mek, and p42
mitogen-activated protein (MAP) kinase can trigger release from
G2-phase arrest in Xenopus oocytes and
oocyte extracts and can cause Xenopus embryos and
extracts to arrest in mitosis. Herein we have found that activation of
the MAP kinase cascade can also bring about an interphase arrest in
cycling extracts. Activation of the cascade early in the cycle was
found to bring about the interphase arrest, which was characterized by
an intact nuclear envelope, partially condensed chromatin, and
interphase levels of H1 kinase activity, whereas activation of the
cascade just before mitosis brought about the mitotic arrest, with a
dissolved nuclear envelope, condensed chromatin, and high levels of H1
kinase activity. Early MAP kinase activation did not interfere
significantly with DNA replication, cyclin synthesis, or association of
cyclins with Cdc2, but it did prevent hyperphosphorylation of Cdc25 and Wee1 and activation of Cdc2/cyclin complexes. Thus, the extracts were
arrested in a G2-like state, unable to activate Cdc2/cyclin complexes. The MAP kinase-induced G2 arrest appeared not to
be related to the DNA replication checkpoint and not to be mediated through inhibition of Cdk2/cyclin E; evidently a novel mechanism underlies this arrest. Finally, we found that by delaying the inactivation of MAP kinase during release of a cytostatic
factor-arrested extract from its arrest state, we could delay the
subsequent entry into mitosis. This finding suggests that it is the
persistence of activated MAP kinase after fertilization that allows the
occurrence of a G2-phase during the first mitotic cell
cycle.
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