{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,30]],"date-time":"2026-03-30T14:32:51Z","timestamp":1774881171117,"version":"3.50.1"},"reference-count":114,"publisher":"Wiley","issue":"19","license":[{"start":{"date-parts":[[2025,9,5]],"date-time":"2025-09-05T00:00:00Z","timestamp":1757030400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["physoc.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Journal of Physiology"],"published-print":{"date-parts":[[2025,10]]},"abstract":"<jats:sec><jats:title>Abstract<\/jats:title><jats:p>At the onset of training, each exercise session transiently shifts the distribution of histone post\u2010transcriptional modifications (HPTMs) to activate genes that drive muscle adaptations. The resulting cyclic changes in gene expression promote the acquisition of high oxidative capacities and gains in capillaries. If training stops or remains at the same intensity, adaptation ceases. Whether silencing HPTMs helps to halt adaptation remains understudied. The E3 ubiquitin ligase murine double minute (MDM2) and enhancer of zester homolog 2 (EZH2) interact and tri\u2010methylate histone H3 on lysine 27 (H3K27<jats:sup>me3<\/jats:sup>), silencing genes. C57Bl6 mice ran for 9\u00a0weeks (5\u00a0days a week) maintaining a constant running speed for the last 5\u00a0weeks of training. Muscles were collected 72\u00a0h after the last run. Training increased MDM2 and EZH2 proteins and led to an H3K27<jats:sup>me3<\/jats:sup> enrichment in <jats:italic>Kdr<\/jats:italic> and <jats:italic>Notch1<\/jats:italic> regulatory sequences<jats:italic>. Kdr<\/jats:italic> mRNA levels decreased, following the canonical model that H3K27<jats:sup>me3<\/jats:sup> silences genes. <jats:italic>Notch1<\/jats:italic> mRNA increased. Trained muscles had greater levels of H3K27<jats:sup>me3<\/jats:sup> detected at 25\u00a0kDa and no change at the expected molecular weight of 17\u00a0kDa. The 25\u00a0kDa band was identified as a ubiquitylated form of H3 (H3<jats:sup>Ub<\/jats:sup>). C2C12 myotubes exposed to four consecutive days of 90\u00a0min electrostimulation had higher levels of H3<jats:sup>Ub<\/jats:sup>. EZH2 inhibition counteracted the electrostimulation\u2010driven accumulation of H3<jats:sup>Ub<\/jats:sup> and increased <jats:italic>Notch1<\/jats:italic> mRNA. Serdemetan, an MDM2 ring domain inhibitor, reduced <jats:italic>Notch1<\/jats:italic> mRNA and H3<jats:sup>Ub<\/jats:sup> level in myotubes. MDM2\u2010dependent ubiquitylation of H3 might upregulate <jats:italic>Notch1<\/jats:italic> when endurance training ceases. The role H3<jats:sup>Ub<\/jats:sup> plays in establishing a new muscle homeostasis remains unclear.\n<jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/tjp70068-gra-0001-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text><\/jats:p><\/jats:sec><jats:sec><jats:title>Key points<\/jats:title><jats:p><jats:list list-type=\"bullet\">\n<jats:list-item><jats:p>Whether epigenetic silencing histone marks play a role once skeletal muscle adaptations have occurred following endurance training remains unclear.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>The E3 ubiquitin ligase MDM2 and the epigenetic writer EZH2 interact to establish H3K27<jats:sup>me3<\/jats:sup> marks that silence genes, and endurance training increased the expression of both proteins.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>After weeks of training new capillaries were established, and lower levels of <jats:italic>Kdr<\/jats:italic> mRNA and increased H3K27<jats:sup>me3<\/jats:sup> marking on <jats:italic>Kdr<\/jats:italic> regulatory sequences question whether silencing of this positive regulator of angiogenesis is required to halt microvascular remodelling.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>Training increases skeletal muscle abundance of a ubiquitylated form of H3 (H3<jats:sup>Ub<\/jats:sup>); in myotubes EZH2 inhibition limits H3<jats:sup>Ub<\/jats:sup> accumulation after contractile activity repeated over 4\u00a0days and MDM2 inhibition reduces H3<jats:sup>Ub<\/jats:sup> levels and upregulates <jats:italic>Notch1<\/jats:italic> expression.<\/jats:p><\/jats:list-item>\n<jats:list-item><jats:p>MDM2\u2010dependent ubiquitylation of H3 might explain why H3K27<jats:sup>me3<\/jats:sup> enrichment fails to silence <jats:italic>Notch1<\/jats:italic> after training; whether H3<jats:sup>Ub<\/jats:sup> is crucial to halt adaptation and establish a new muscle homeostasis requires further investigation.<\/jats:p><\/jats:list-item>\n<\/jats:list><\/jats:p><\/jats:sec>","DOI":"10.1113\/jp288947","type":"journal-article","created":{"date-parts":[[2025,9,5]],"date-time":"2025-09-05T19:25:16Z","timestamp":1757100316000},"page":"5477-5508","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Endurance training increases a ubiquitylated form of histone H3 in the skeletal muscle, supporting <i>Notch1<\/i> upregulation in an MDM2\u2010dependent manner"],"prefix":"10.1113","volume":"603","author":[{"given":"Brian","family":"Lam","sequence":"first","affiliation":[{"name":"Angiogenesis Research Group, School of Kinesiology and Health Science and the Muscle Health Research Centre, Faculty of Health York University  Toronto Ontario 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