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Tripartite motif-containing protein 10 (TRIM10) is a member of the TRIM family, characterized by an N-terminal RING finger, B-box zinc finger domains, and a coiled-coil region. As an E3 ubiquitin ligase, TRIM10 is implicated in protein quality control, differentiation, and survival of terminal erythroid cells. It regulates cardiac hypertrophy by promoting ubiquitination and degradation of PTEN, leading to AKT signaling activation. TRIM10 also modulates immune response by repressing STAT1/STAT2 phosphorylation in the JAK/STAT pathway. Elevated TRIM10 has been observed in pathological cardiac hypertrophy, suggesting its potential as a therapeutic target and biomarker in cardiovascular disease.
Drugs targeting E3 ligases generally act by modulating substrate ubiquitination, but no specific mechanism for TRIM10-targeting drugs is documented
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