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Regulation of G(2)/M events by Cdc25A through phosphorylation-dependent modulation of its stability
N Mailand, AV Podtelejnikov, A Groth, M Mann, J Bartek, J Lukas
Jazyk angličtina Země Anglie, Velká Británie
NLK
Free Medical Journals
od 1982 do Před 1 rokem
PubMed Central
od 1982
Europe PubMed Central
od 1982 do Před 1 rokem
ProQuest Central
od 2000-01-04 do 2013-12-11
Open Access Digital Library
od 1997-01-01
Open Access Digital Library
od 1997-01-01
Medline Complete (EBSCOhost)
od 1997-01-02 do Před 1 rokem
Health & Medicine (ProQuest)
od 2000-01-04 do 2013-12-11
Public Health Database (ProQuest)
od 2000-01-04 do 2013-12-11
Wiley Free Content
od 1997 do Před 1 rokem
PubMed
12411508
Knihovny.cz E-zdroje
- MeSH
- cyklin B metabolismus MeSH
- fosfatasy cdc25 chemie metabolismus MeSH
- fosforylace MeSH
- G2 fáze * MeSH
- lidé MeSH
- mitóza * MeSH
- molekulární sekvence - údaje MeSH
- poškození DNA MeSH
- proteinkinasa CDC2 metabolismus MeSH
- sekvence aminokyselin MeSH
- serin metabolismus MeSH
- stabilita enzymů MeSH
- ubikvitin metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
DNA replication in higher eukaryotes requires activation of a Cdk2 kinase by Cdc25A, a labile phosphatase subject to further destabilization upon genotoxic stress. We describe a distinct, markedly stable form of Cdc25A, which plays a previously unrecognized role in mitosis. Mitotic stabilization of Cdc25A reflects its phosphorylation on Ser17 and Ser115 by cyclin B-Cdk1, modifications required to uncouple Cdc25A from its ubiquitin-proteasome-mediated turnover. Cdc25A binds and activates cyclin B-Cdk1, accelerates cell division when overexpressed, and its downregulation by RNA interference (RNAi) delays mitotic entry. DNA damage-induced G(2) arrest, in contrast, is accompanied by proteasome-dependent destruction of Cdc25A, and ectopic Cdc25A abrogates the G(2) checkpoint. Thus, phosphorylation-mediated switches among three differentially stable forms ensure distinct thresholds, and thereby distinct roles for Cdc25A in multiple cell cycle transitions and checkpoints.
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- $a DNA replication in higher eukaryotes requires activation of a Cdk2 kinase by Cdc25A, a labile phosphatase subject to further destabilization upon genotoxic stress. We describe a distinct, markedly stable form of Cdc25A, which plays a previously unrecognized role in mitosis. Mitotic stabilization of Cdc25A reflects its phosphorylation on Ser17 and Ser115 by cyclin B-Cdk1, modifications required to uncouple Cdc25A from its ubiquitin-proteasome-mediated turnover. Cdc25A binds and activates cyclin B-Cdk1, accelerates cell division when overexpressed, and its downregulation by RNA interference (RNAi) delays mitotic entry. DNA damage-induced G(2) arrest, in contrast, is accompanied by proteasome-dependent destruction of Cdc25A, and ectopic Cdc25A abrogates the G(2) checkpoint. Thus, phosphorylation-mediated switches among three differentially stable forms ensure distinct thresholds, and thereby distinct roles for Cdc25A in multiple cell cycle transitions and checkpoints.
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