Ubiquitin carboxyl-terminal hydrolase 37 (UCH37)

Ubiquitin carboxyl-terminal hydrolase 37 (UCH37, also called UCHL5 or UCH-37) is a deubiquitinating enzyme that plays a key role in the regulation of protein turnover by removing ubiquitin from the distal end of polyubiquitin chains, with specificity mainly for Lys48-linked polyubiquitin[1][3][5]. It is a member of the UCH/Deubiquitinating enzyme (DUB) family. UCH37’s catalytic activity is regulated by interaction with proteasome subunits (notably hRpn13/ADRM1), which activates the enzyme, or with chromatin remodeling factors (e.g., NFRKB/INO80G), which inhibit it[3][5]. UCH37 has recognized roles in proteasomal degradation, cell proliferation, apoptosis, and is highly conserved among eukaryotes. Aberrant expression or activity is implicated in oncogenesis, tumor cell invasion, and progression, as well as in neurodegenerative and fibrotic diseases, making it a focus for targeted cancer drug development[1][3][5].

Other names

UCHL5UCH-37

Inhibitors would block the deubiquitinating (isopeptidase) activity, leading to increased protein degradation via the ubiquitin-proteasome system and potential induction of apoptosis in cancer cells[1][3][5].