Ubiquitin carboxyl-terminal hydrolase 27 (USP27X)

Ubiquitin carboxyl-terminal hydrolase 27 (USP27X) is a member of the ubiquitin-specific protease (USP) family of deubiquitinating enzymes. USP27X cleaves ubiquitin from substrate proteins, particularly removing Lys48-linked polyubiquitin to prevent proteasome-mediated degradation. Key substrates include the pro-apoptotic protein Bim, the chromatin regulator CBX2, and components of cell proliferation and immune signaling pathways. USP27X plays crucial roles in apoptosis (by stabilizing Bim), regulation of cell proliferation and invasion (by stabilizing CBX2), transcription (via histone H2B deubiquitination), and innate immunity (by stabilizing cGAS in the cGAS-STING pathway). Mutations in USP27X are linked to X-linked intellectual disability syndromes. Both loss and gain of USP27X function are implicated in cancer, with context-dependent effects either promoting cell death (tumor suppression) or supporting tumor growth and metastasis (oncogenic function depending on substrate and cell type)[1][2][3][4].

Other names

USP27Deubiquitinating enzyme 27Ubiquitin-specific-processing protease 27Ubiquitin thioesterase 27Ubiquitin carboxyl-terminal hydrolase 22-likeMRX105USP22LXLID105

Inhibitors would be expected to block DUB (deubiquitinating) activity, impeding substrate stabilization - No small-molecule drugs with direct action on USP27X described in current literature