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Phosphorylation of histone H2A.X as a DNA‑associated biomarker (Review)

. The complex genomic structure of eukaryotic cells is primarily achieved by the binding of DNA to histones. Different members of the histone families form a complex with genomic DNA and, as a nucleosome, constitute the functional unit of chromatin. In addition to their structural functionality, histones are also involved in other molecular mechanisms, such as DNA damage recognition and repair. A very important factor of DNA damage management is the histone H2A.X. The phosphorylation of H2A.X initiates various processes of the DNA repair systems and plays significant roles in cellular regu‑ lation. The H2A.X phosphorylation status represents a central sum parameter for genome integrity and allows conclusions to be drawn about DNA‑associated processes in cells and tissues. As a biomarker for DNA damage and genotoxicity, as well as a clinical marker for radiotherapy outcome, drug efficacy and tissue regeneration, the H2A.X phosphorylation status repre‑ sents an effective biomarker for current and future biomedical applications. The present brief review article provides an over‑ view of the various molecular functions and cellular events in which the phosphorylation of histone H2A.X can occur. reflects the enormous efficiency of the DNA damage detection and repair system of eukaryotic cells (11). The phosphorylation of H2AX serves as one of the first signals for a DSB, and is thus an essential prerequisite for the activation of DNA repair systems, and thus contributes significantly to the stabilization of the genome against genotoxic noxae. A single DSB leads to the binding of several hundred to thousand γ H2A.X proteins to the affected DNA region.