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Wip1 phosphatase is associated with chromatin and dephosphorylates gammaH2AX to promote checkpoint inhibition
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SYSNO ASEP 0354924 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Wip1 phosphatase is associated with chromatin and dephosphorylates gammaH2AX to promote checkpoint inhibition Tvůrce(i) Macůrek, Libor (UMG-J) RID, ORCID
Lindqvist, A. (NL)
Voets, O. (NL)
Kool, J. (NL)
Vos, H.R. (NL)
Medema, R.H. (NL)Zdroj.dok. Oncogene. - : Springer - ISSN 0950-9232
Roč. 29, č. 15 (2010), s. 2281-2291Poč.str. 11 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova DNA damage ; checkpoint ; phosphatase Vědní obor RIV EB - Genetika a molekulární biologie CEP GPP305/10/P420 GA ČR - Grantová agentura ČR CEZ AV0Z50520514 - UMG-J (2005-2011) UT WOS 000276685200013 DOI 10.1038/onc.2009.501 Anotace DNA double-stranded breaks (DSBs) elicit a checkpoint response that causes a delay in cell cycle progression and enables DNA repair. Phosphorylated form of the histone H2AX (called gamma-H2AX) serves as an essential platform for recruitment and retention of additional components of the checkpoint signaling cascade (such as MDC1 and 53BP1) in the chromatin region flanking the DSB. Here we demonstrate that the Wip1 phosphatase is bound to chromatin and directly dephosphorylates gamma-H2AX. Cells depleted of Wip1 fail to dephosphorylate gamma-H2AX during checkpoint recovery. Conversely, premature activation of Wip1 leads to displacement of MDC1 from damage foci and prevents activation of the checkpoint. Taken together, our data demonstrate that Wip1 plays an essential role in dephosphorylation of gamma-H2AX in order to silence the checkpoint and restore chromatin structure once DNA damage is repaired. Pracoviště Ústav molekulární genetiky Kontakt Nikol Škňouřilová, nikol.sknourilova@img.cas.cz, Tel.: 241 063 217 Rok sběru 2011
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