Abstract:
The ubiquitin proteasome system (UPS), which mediates the degradation of more than 80% proteins in eukaryotic cells, plays a crucial role in orchestrating the stabilization and function of substrates. As a key regulator of ubiquitination, deubiquitinating enzymes (DUBs) could cleave ubiquitin from the substrates, modify ubiquitin chains and process ubiquitin precursors, which is associated with various physiological and pathological processes. Among these DUBs, proteasome 26S subunit non-ATPase 14 (PSMD14) is a component of proteasome 26S subunit without ATPase activity, whose effects on tumorigenesis and progression are paid more and more attention to. Here, the research progress on the expressions, mechanisms and inhibitors of PSMD14 in human cancers is reviewed in this paper.