Chaperone-driven proteasome assembly.
Assembly of the 34-subunit, 2.5 MDa 26S proteasome is a carefully choreographed intricate process. It starts with formation of a seven-membered alpha-ring that serves as a template for assembly of the complementary beta-ring-forming 'half-proteasomes'. Dimerization results in a latent 20S core particle that can serve further as a platform for 19S regulatory particle attachment and formation of the biologically active 26S proteasome for ubiquitin-dependent proteolysis. Both general and dedicated proteasome assembly chaperones regulate the efficiency and outcome of critical steps in proteasome biogenesis, and in complex association.
Rosenzweig
Rina
R
Department of Biology, Technion - Israel Institute of Technology, 32000 Haifa, Israel.
Glickman
Michael H
MH
D019281:Dimerization; D054641:Dual Specificity Phosphatase 2 / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry / Q000378:metabolism*; D020836:Protein Structure, Quaternary; D021122:Protein Subunits / Q000737:chemistry / Q000378:metabolism*
D018832:Molecular Chaperones; D021122:Protein Subunits; C110856:proteasome maturation protein; D054641:Dual Specificity Phosphatase 2; D046988:Proteasome Endopeptidase Complex