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Graphical Abstract Highlights d H2AX is degraded via poly-ubiquitination mediated by HUWE1 d H2AX is transiently stabilized upon DSB formation to efficiently form gH2AX foci d H2AX stabilization is mediated by ATM, SIRT6, and SNF2H SUMMARY In response to DNA double-strand breaks (DSBs), H2AX is rapidly phosphorylated at Ser139 to promote DSB repair. Here we show that H2AX is rapidly stabilized in response to DSBs to efficiently generate gH2AX foci. This mechanism operated even in quiescentdoi:10.1016/j.celrep.2015.11.054 pmid:26711340 fatcat:yxuaja2nbfe7pmalmd5uowzvtq