Reactome | Formation of the outer ring of the 20S core particle

Formation of the outer ring of the 20S core particle

Stable Identifier

R-HSA-9907912

Type

Reaction [binding]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

3/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Formation of the outer ring of the 20S core particle

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

The outer ring of 20S core particle (20S CP) of 26S proteasome consist of seven different alpha subunits (alpha1-7, PSMA1-7 officially in humans, where alpha-1 corresponds to PSMA6, alpha-2 to PSMA2, alpha-3 to PSMA4, alpha-4 to PSMA7, alpha-5 to PSMA5, alpha-6 to PSMA1, and alpha-7 to PSMA3) (reviewed in Tomko and Hochstrasser 2013). The PSMA5 (alpha-5) subunit is pre-bound to the proteasome chaperone dimer PSMG3:PSMG4 (Satoh et al. 2019), and PSMG3:PSMG4 is needed for efficient and accurate outer ring assembly (Hirano et al. 2006). In human embryonic kidney cell line 293 (HEK293), the knockdown of PSMG3 increases the level of free forms of alpha subunits (Hirano et al. 2006).

Literature References

PubMed ID	Title	Journal	Year
17189198	Cooperation of multiple chaperones required for the assembly of mammalian 20S proteasomes Kasahara, M, Murata, S, Natsume, T, Hirano, Y, Kishimoto, T, Hendil, KB, Tanaka, K, Iemura, S, Niwa, S, Hayashi, H	Mol Cell	2006
31067643	Molecular and Structural Basis of the Proteasome α Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer Yagi-Utsumi, M, Kurimoto, E, Tanaka, K, Satoh, T, Okamoto, K, Kato, K	Int J Mol Sci	2019