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Journal Club
DNA Damage Response: Determining the Fate of Phosphorylated Histone H2AX
Jonathan Rios-Doria, Alyson Fay, Aneliya Velkova and Alvaro N.A. Monteiro
volume 5 | issue 2
february 2006Pages: 142-144
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Phosphorylation of histone H2AX at Serine 139 is one of the earliest events after DNA damage and is required for the retention of factors involved in repair at the site of the break. Intriguingly, H2AX phosphorylation spreads from the vicinity of the break to both directions spanning large chromosomal regions. Phosphorylated H2AX (also known as ?-H2AX) then progressively disappears with kinetics that correlates with the completion of DNA repair. Despite intense investigation on the kinases and stimuli involved in ?-H2AX formation, the mechanism of ?-H2AX disappearance has remained obscure. Three recent papers shed light on this process and suggest that H2AX may serve as a signaling platform that integrates repair and cell cycle checkpoints.
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDFIf the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.