E3 ubiquitin-protein ligase TRIM32 (TRIM32)

E3 ubiquitin-protein ligase TRIM32 (TRIM32) is an enzyme responsible for tagging proteins with ubiquitin and targeting them for degradation in the proteasome, influencing cellular protein turnover, signaling, and homeostasis[3][1][7]. Structurally, TRIM32 contains a RING finger, B-box domain, coiled-coil region, and six C-terminal NHL repeats—each contributing to its catalytic and substrate recognition functions[1][3][5]. Biologically, TRIM32 is widely expressed, regulates muscle and neural cell fate decisions, impacts apoptosis by degrading anti-apoptotic proteins (such as XIAP), mediates innate immunity, and supports glucose metabolism in growing tissues[5][7]. Pathologically, mutations in TRIM32 are causative for limb-girdle muscular dystrophy type 2H (LGMD2H), sarcotubular myopathy, and Bardet-Biedl syndrome 11, and are implicated in certain cancers with altered expression or function[2][4][8][5]. Currently, TRIM32 is considered a potential therapeutic target but no approved drugs directly act on it; its biomarker utility resides in genetic diagnosis and muscle pathology[2][4][7]. Manipulation of TRIM32 activity carries notable risks due to its crucial role in tissue maintenance and organ function.

Other names

Tripartite motif containing 32TATIPBBS1172 kDa Tat-interacting proteinRING-type E3 ubiquitin transferase TRIM32Zinc finger protein HT2ALGMD2HLGMDR8TAT-interactive proteinThin (Drosophila homolog)

E3 ligase inhibition or modulation (inferred, as no drugs directly reported[7]). Sensitization to apoptosis via antagonism of XIAP (experimentally observed, not clinical)[5].