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PMID: 9362060 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Induction of a G2-phase arrest in Xenopus egg extracts by activation of p42 mitogen-activated protein kinase.

Molecular biology of the cell ·Vol. 8 ·No. 11 ·1997-11-00 ·Pages 2157-69

Walter SA, Guadagno TM, Ferrell JE

Abstract

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.

MeSH Terms
Animals CDC2 Protein Kinase/metabolism CDC2-CDC28 Kinases Cell Cycle Proteins/metabolism Cell Extracts Chromatin/metabolism Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinases/metabolism,pharmacology Cyclins/metabolism DNA Replication/physiology Enzyme Activation G2 Phase/physiology Mitogen-Activated Protein Kinase 1/metabolism Mitosis/physiology Nuclear Envelope/metabolism Nuclear Proteins Oocytes Phosphoprotein Phosphatases/metabolism Phosphorylation Protamine Kinase/metabolism Protein Serine-Threonine Kinases/metabolism,pharmacology Protein-Tyrosine Kinases/metabolism Proto-Oncogene Proteins c-mos/pharmacology Recombinant Proteins/pharmacology Time Factors Xenopus Xenopus Proteins cdc25 Phosphatases
Chemicals
Cell Cycle Proteins Cell Extracts Chromatin Cyclins Nuclear Proteins Recombinant Proteins Xenopus Proteins WEE1 protein, Xenopus Protein-Tyrosine Kinases Protamine Kinase Protein Serine-Threonine Kinases Proto-Oncogene Proteins c-mos CDC2 Protein Kinase CDC2-CDC28 Kinases Cdk2 protein, Xenopus Cyclin-Dependent Kinase 2 Cyclin-Dependent Kinases Mitogen-Activated Protein Kinase 1 Phosphoprotein Phosphatases cdc25 Phosphatases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Walter S A
Department of Molecular Pharmacology, Stanford University School of Medicine, California 94305-5332, USA.
Guadagno T M
Ferrell J E
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Article Info
Journal
Molecular biology of the cell
Abbr.
Mol Biol Cell
ISSN
1059-1524
DOI
10.1091/mbc.8.11.2157
Published
1997-11-00
Pages
2157-69
Language
English
Region
United States
NLM ID
9201390
PMCID
PMC25699
Subset
IM
Grants
NIGMS NIH HHS · GM-46383 · United States
External Links
PubMed source DOI: 10.1091/mbc.8.11.2157 PMC Full Text View journal details
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