Ubiquitin carboxyl-terminal hydrolase 17-like protein 23 (USP17L23)

Ubiquitin carboxyl-terminal hydrolase 17-like protein 23 (USP17L23) is a member of the USP17 subfamily of deubiquitinating enzymes (DUBs), which are cysteine proteases that remove ubiquitin from protein substrates[2][7]. The USP17 family is characterized by the presence of a USP domain responsible for deubiquitinating activity, and many members (but not all) also possess hyaluronan- and RNA-binding motifs that modulate their subcellular localization and function[1][2]. USP17L23, like related subfamily members, is predicted to localize to the nucleus and endoplasmic reticulum[7], and is implicated in the regulation of cell proliferation, cell cycle, apoptosis, and immune responses, including Th17-mediated immunity[1][2][3][4][5]. It modulates the stability and activity of multiple cellular proteins via deubiquitination, affecting signaling pathways involved in cancer, inflammation, and autoimmunity[1][3][4][5]. USP17 family proteins are being explored as potential therapeutic targets, particularly for cancer and inflammatory disorders, though no direct specificity for USP17L23 in clinical drug development has yet been demonstrated.

Other names

USP17L23Ubiquitin specific peptidase 17 like family member 23Ubiquitin carboxyl-terminal hydrolase 17-like protein 23U17LN (GeneCards)[Ensembl: ENSG00000250913][7][NCBI Gene: 101241878][7][HGNC: 44451][7]

Not established for USP17L23-specific inhibitors. For DUB inhibitors more broadly: - Inhibit enzymatic deubiquitination, leading to accumulation of ubiquitinated substrates and altered degradation or signaling (mechanism is substrate- and context-dependent)[3][5].