POMP binds the 20S core particle outer ring

Stable Identifier
R-HSA-9908069
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
3/5
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POMP (UMP1), proteasome maturation protein which may function as a homotetramer (Hoefer et al. 2006), binds the formed outer ring (Hirano et al. 2006). Binding of POMP to the outer ring is mutually exclusive with binding of PSMG3:PSMG4 dimer to the outer ring (Hirano et al. 2006), although a transient interaction between PSMG3:PSMG4 and POMP was detected by the analysis of 20S core particle intermediates (Adolf et al. 2024). Dissociation of PSMG3 from the outer ring during formation of half-proteasomes was reported in human cells (Hirano et al. 2006) and shown to happen after the incorporation of beta-3 (PSMB3) (Hirano et al. 2008). POMP initiates the assembly of the inner ring. Beta subunits (PSMBs) of the inner ring assemble onto the inner surface of outer ring. POMP may help prevent the premature dimerization of precursors containing incomplete sets of beta subunits (reviewed in Tomko and Hochstrasser 2013).
Literature References
PubMed ID Title Journal Year
17189198 Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes

Hirano, Y, Hayashi, H, Iemura, S, Hendil, KB, Niwa, S, Kishimoto, T, Kasahara, M, Natsume, T, Tanaka, K, Murata, S

Mol Cell 2006
38600324 Visualizing chaperone-mediated multistep assembly of the human 20S proteasome

Adolf, F, Du, J, Goodall, EA, Walsh, RM, Rawson, S, von Gronau, S, Harper, JW, Hanna, J, Schulman, BA

Nat Struct Mol Biol 2024
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