DNA damage response: determining the fate of phosphorylated histone H2AX.
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 gamma-H2AX) then progressively disappears with kinetics that correlates with the completion of DNA repair. Despite intense investigation on the kinases and stimuli involved in gamma-H2AX formation, the mechanism of gamma-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.
Risk Assessment, Detection and Intervention Program, The H. Lee Moffitt Cancer Center & Research Institute, Tampa, Florida 33612, USA.
Jonathan
J
Rios-Doria
Alyson
A
Fay
Aneliya
A
Velkova
Alvaro N A
AN
Monteiro
D000818:Animals; D002453:Cell Cycle; D004249:DNA Damage; D004260:DNA Repair; D006657:Histones / Q000378:metabolism*; D010766:Phosphorylation; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism; D012694:Serine / Q000378:metabolism
D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; C507778:gammaH2AX protein, S cerevisiae; D012694:Serine