Proteasome maturation protein (POMP)

Proteasome maturation protein (POMP) is a short-lived, non-enzymatic assembly chaperone required for the construction of the 20S core proteasome complex in all eukaryotic cells[1][2][3]. POMP localizes primarily to the endoplasmic reticulum (ER), where it interacts with proteasome precursor complexes, recruiting β subunits to the α-ring in a stepwise manner and guiding their proper insertion to form a half-proteasome[2][3]. After β-ring completion and dimerization of two half-proteasomes, POMP orchestrates the maturation checkpoint by ensuring activation and cleavage of the catalytic β subunits; once cleavage occurs, POMP itself is targeted for proteolysis and removed, enabling the mature proteasome to assume its full degradative capacity[1][3]. This stepwise process is vital for cellular protein turnover, controlling degradation of misfolded, damaged, or regulatory proteins, and is critically involved in cell cycle, immune response, and adaptation to stress. Disease-associated mutations, especially in autoinflammatory syndromes (such as PRAAS2), have revealed POMP’s essential role in proteostasis and immune system function[2]. No drugs currently directly target POMP, but its dysregulation can profoundly affect cellular viability and homeostatic pathways, positioning it as a molecular target of research interest in cancer, neurodegeneration, immune disorders, and aging[1][2][3].

Other names

UMP1C13orf12HSPC014HSPC036PNAS-110hUMP1ProteassemblinProtein UMP1 homologPRAAS22510048O06Rik

No current drugs directly target POMP; proteasome inhibitors impede proteasome function downstream of POMP’s action.