TRIM17 is an E3 ubiquitin ligase expressed at low levels in most adult tissues but highly induced under stress conditions, functioning as a cellular stress sensor 1. Its primary function involves regulating neuronal apoptosis, autophagy, and cell proliferation through substrate ubiquitination and proteasomal degradation 1. TRIM17 mediates neuronal death by ubiquitinating and degrading the anti-apoptotic protein MCL1 1, while also inhibiting NFAT transcription factors NFATC3 and NFATC4 by blocking their nuclear localization 2. Uniquely, TRIM17 possesses dual functionality: it stabilizes certain proteins by inhibiting other TRIM E3 ligases, exemplified by blocking TRIM28-mediated ubiquitination of BCL2A1 3. In autophagy regulation, TRIM17 assembles MCL1 with BECN1 to inhibit autophagic degradation of specific targets while promoting midbody autophagy 1. Clinically, TRIM17 upregulation associates with poor prognosis in multiple cancers including osteosarcoma, gastric cancer, and non-small cell lung cancer, where it promotes tumor progression, chemoresistance, and cell survival by degrading pro-apoptotic proteins like BAX and RBM38 4, 5, 6. Additionally, TRIM17 dysfunction is implicated in Parkinson's disease pathogenesis through regulation of α-synuclein transcription via the ZSCAN21 pathway 7.