Assembly, structure, and function of the 26S proteasome.
The 26S proteasome is a large multiprotein complex involved in the regulated degradation of ubiquitinated proteins in the cell. The 26S proteasome has been shown to control an increasing number of essential biochemical mechanisms of the cellular lifecycle including DNA synthesis, repair, transcription, translation, and cell signal transduction. Concurrently, it is increasingly seen that malfunction of the ubiquitin proteasome system contributes to the pathogenesis of disease. The recent identification of four molecular chaperones, in addition to five previously identified chaperones, have provided mechanistic insight into how this cellular megastructure is assembled in the cell. These data, together with new insights into the structure and function of the proteasome, provide a much better understanding of this complex protease.
Bedford
Lynn
L
School of Biomedical Sciences, University of Nottingham Medical School, Nottingham, UK.
Paine
Simon
S
Sheppard
Paul W
PW
Mayer
R John
RJ
Roelofs
Jeroen
J
D000818:Animals; D002468:Cell Physiological Phenomena; D006801:Humans; D018832:Molecular Chaperones / Q000032:analysis; D046988:Proteasome Endopeptidase Complex / Q000737:chemistry* / Q000378:metabolism*; D057149:Ubiquitinated Proteins / Q000378:metabolism
D018832:Molecular Chaperones; D057149:Ubiquitinated Proteins; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease