Wild-type p53-induced Phosphatase 1 Dephosphorylates Histone Variant γ-H2AX and Suppresses DNA Double Strand Break Repair

• DOI: 10.1074/jbc.m109.071696
• Publication Date: 2010-01-30T04:00:20Z
• Authors: Sung-Hwan Moon; Lin Lin; Xinna Zhang; Thuy-Ai Nguyen; Yolanda Darlington; Alan S. Waldman; Xiongbin Lu; Lawrence A. Doneh...
• Keywords: Dephosphorylation; Nijmegen breakage syndrome

In response to DNA double strand breaks, the histone variant H2AX at break site is phosphorylated serine 139 by damage sensor kinases such as ataxia telangiectasia-mutated, forming gamma-H2AX. This phosphorylation event critical for sustained recruitment of other proteins repair break. After repair, restoration cell a prestress state associated with gamma-H2AX dephosphorylation and dissolution gamma-H2AX-associated foci. The phosphatases PP2A PP4 have previously been shown dephosphorylate Here, we demonstrate that wild-type p53-induced phosphatase 1 (WIP1) also dephosphorylates in vitro vivo. Overexpression WIP1 reduces formation foci ionizing ultraviolet radiation blocks MDC1 (mediator checkpoint 1) 53BP1 (p53 binding protein Finally, these inhibitory effects on are accompanied suppression repair. Thus, has homeostatic role reversing telangiectasia-mutated H2AX.