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Background:Histones are basic nuclear proteins that form nucleosomes, the fundamental repeating units of eukaryotic chromatin. The N‑terminal tail of histone H3 is subjected to various post‑translational modifications. H3S10p (phosphorylation of histone H3 at Serine 10) is a well‑characterized cell‑cycle‑dependent histone phosphorylation mark. H3S10 is predominantly phosphorylated by Aurora‑B kinase during mitosis. H3S10 phosphorylation plays pivotal roles in mitotic chromatin remodeling. Upon entry into M‑phase, H3S10p massively accumulates along condensed chromosomes. This phosphorylation weakens the interaction between histone H3 and heterochromatin protein HP1, triggering HP1 dissociation from mitotic chromosomes, which is essential for proper chromosome condensation, sister‑chromatid resolution and faithful chromosome segregation. In interphase cells, H3S10p also participates in immediate‑early gene transcriptional activation in response to extracellular stimuli. Crosstalk exists between H3S10 phosphorylation and neighboring acetylation or methylation marks, coordinating chromatin state and gene output. Dysregulation of H3S10p correlates with mitotic defects, chromosome mis‑segregation, genomic instability and oncogenic transformation.
