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Ubiquitination, a classical post\u2010translational modification that regulates protein function and degradation, plays a crucial role in cardiac hypertrophy. In this study, the E3 ubiquitin ligase ring finger protein 115 (RNF115) is identified as a key pro\u2010hypertrophic factor. RNF115 expression is significantly elevated in heart tissues from patients with heart failure, in mice subjected to transverse aortic constriction (TAC) surgery, and in cardiomyocytes treated with angiotensin II (Ang II). RNF115 knockdown attenuates Ang II\u2010induced cardiomyocyte hypertrophy in vitro, whereas cardiomyocyte\u2010specific RNF115 knockout protects against TAC\u2010induced cardiac hypertrophy and dysfunction in vivo. Mechanistically, upregulation of RNF115 promotes the ubiquitination and degradation of spectrin \u03b2, non\u2010erythrocytic 1 (SPTBN1), causing filamentous actin (F\u2010actin) depolymerization, thereby inactivates the Hippo\u2010Yes associated protein (YAP) pathway and drives pro\u2010hypertrophic gene expression. DTD (dithiocarbamate disulfide derivatives) is a potent inhibitor of RNF115 that suppresses SPTBN1 degradation and exerts a protective role in cardiac hypertrophy, indicating that inhibition of RNF115 may represent a potential therapeutic strategy for pathological cardiac hypertrophy and heart failure.<\/jats:p>","DOI":"10.1002\/advs.76077","type":"journal-article","created":{"date-parts":[[2026,6,15]],"date-time":"2026-06-15T11:43:08Z","timestamp":1781523788000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The E3 Ligase RNF115 Aggravates Pathological Cardiac Hypertrophy via Ubiquitin\u2010Mediated Degradation of SPTBN1"],"prefix":"10.1002","volume":"13","author":[{"ORCID":"https:\/\/orcid.org\/0009-0004-3026-3212","authenticated-orcid":false,"given":"Yan","family":"Zu","sequence":"first","affiliation":[{"name":"Key Laboratory of Drug Targets and Translational Medicine For Cardio\u2010cerebrovascular Diseases 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