Ubiquitin specific peptidase 46 (USP46)

Ubiquitin specific peptidase 46 (USP46) is a member of the ubiquitin-specific protease family—enzymes that remove ubiquitin moieties from substrate proteins, reversing ubiquitination and thereby playing a critical role in regulating protein degradation, signal transduction, transcription, and DNA repair. USP46 has a conserved catalytic triad typical of cysteine proteases and regulates neural function, synaptic receptor stability (including AMPA and glutamate receptors), and cell proliferation. It is highly expressed in the brain and has drawn research attention for its involvement in cancer, neurodegenerative and psychiatric disorders. The enzyme acts as a potential therapeutic target, but the precise functional and clinical implications are still under investigation[1][2][4][5][6].

Other names

UBP46USP46 (human gene symbol)

Inhibitors of USP46 would block its deubiquitinating activity and thus promote proteasomal degradation of its substrates, affecting cellular processes such as protein turnover, cell cycle progression, and synaptic plasticity[2].