Ubiquitin specific peptidase 34 (USP34)

Ubiquitin specific peptidase 34 (USP34) is a large cysteine protease within the deubiquitinating enzyme family, characterized by its ability to cleave ubiquitin from protein substrates. It is implicated in multiple cellular processes, including regulation of the canonical Wnt signaling pathway by deubiquitinating and stabilizing AXIN1 and AXIN2, modulation of DNA double-strand break repair through stabilization of RNF168 and histone ubiquitination, and regulation of GPCR signaling by affecting the mRNA expression and cell surface abundance of receptors such as PAR1. USP34 is predominantly localized in the cytosol and nucleus, and its dysfunction has been associated with cancer, neurodevelopmental disorders, and altered osteogenesis. No clinically approved drugs are known to directly target USP34 as of the most recent literature.

Other names

Ubiquitin carboxyl-terminal hydrolase 34KIAA0570KIAA0729Deubiquitinating enzyme 34Ubiquitin thioesterase 34Ubiquitin-specific-processing protease 34ubiquitin specific protease 34

Inhibitors of USP34 would block its deubiquitinating activity, potentially destabilizing or degrading target proteins such as AXIN1/2. Modulation of the DNA damage response through interference with histone or protein ubiquitination.