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Polo-like kinase 1 inhibits DNA damage response during mitosis
J. Benada, K. Burdová, T. Lidak, P. von Morgen, L. Macurek,
Jazyk angličtina Země Spojené státy americké
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 2002 do Před 1 rokem
PubMed Central
od 2009 do Před 1 rokem
Europe PubMed Central
od 2009 do Před 1 rokem
- MeSH
- fosforylace MeSH
- HeLa buňky MeSH
- histony metabolismus MeSH
- intracelulární signální peptidy a proteiny antagonisté a inhibitory chemie metabolismus MeSH
- kinetochory metabolismus MeSH
- lidé MeSH
- malá interferující RNA metabolismus MeSH
- mitóza * MeSH
- nádorové buněčné linie MeSH
- oprava DNA * MeSH
- poškození DNA účinky záření MeSH
- protein-serin-threoninkinasy antagonisté a inhibitory genetika metabolismus MeSH
- proteinkinasa CDC2 metabolismus MeSH
- proteiny buněčného cyklu antagonisté a inhibitory genetika metabolismus MeSH
- protoonkogenní proteiny antagonisté a inhibitory genetika metabolismus MeSH
- RNA interference MeSH
- terciární struktura proteinů MeSH
- ubikvitinace MeSH
- záření gama MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
In response to genotoxic stress, cells protect their genome integrity by activation of a conserved DNA damage response (DDR) pathway that coordinates DNA repair and progression through the cell cycle. Extensive modification of the chromatin flanking the DNA lesion by ATM kinase and RNF8/RNF168 ubiquitin ligases enables recruitment of various repair factors. Among them BRCA1 and 53BP1 are required for homologous recombination and non-homologous end joining, respectively. Whereas mechanisms of DDR are relatively well understood in interphase cells, comparatively less is known about organization of DDR during mitosis. Although ATM can be activated in mitotic cells, 53BP1 is not recruited to the chromatin until cells exit mitosis. Here we report mitotic phosphorylation of 53BP1 by Plk1 and Cdk1 that impairs the ability of 53BP1 to bind the ubiquitinated H2A and to properly localize to the sites of DNA damage. Phosphorylation of 53BP1 at S1618 occurs at kinetochores and in cytosol and is restricted to mitotic cells. Interaction between 53BP1 and Plk1 depends on the activity of Cdk1. We propose that activity of Cdk1 and Plk1 allows spatiotemporally controlled suppression of 53BP1 function during mitosis.
Academy of Sciences of the Czech Republic
Department of Cancer Cell Biology
Citace poskytuje Crossref.org
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