Ontology highlight
ABSTRACT: Background
With aging, the canonical histone H3.1/3.2 in skeletal muscle is progressively replaced by the non-canonical variant H3.3. Although H3.3 is thought to be involved in age-related epigenetic regulation due to its role as a histone variant, its functional characteristics remain largely unknown. Serine 31 (S31) is a unique amino acid residue of H3.3 that undergoes phosphorylation. Therefore, the present study aimed to investigate the relationship between skeletal muscle aging and H3.3 phosphorylation at S31 (H3.3S31ph).Results
We first demonstrated that H3.3S31ph levels were significantly reduced in the tibialis anterior muscle of 75-wk-old mice compared to 8-wk-old mice. We then examined the effects of viral vector-mediated expression of wild-type H3.3 or a phosphor
SUBMITTER: Maruyama S
PROVIDER: S-EPMC12459025 | biostudies-literature | 2025 Sep
REPOSITORIES: biostudies-literature