Structure characterization of the 26S proteasome

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In all eukaryotic cells, 26S proteasome plays an essential role in the process of ATP-dependent protein degradation. In this review, we focus on structure characterization of the 26S proteasome. Although the progress towards a high-resolution structure of the 26S proteasome has been slow, the recently solved structures of various proteasomal subcomplexes have greatly enhanced our understanding of this large machinery. In addition to having an ATP-dependent proteolytic function, the 26S proteasome is also involved in many non-proteolytic cellular activities, which are often mediated by subunits in its 19S regulatory complex. Thus, we include a detailed discussion of the structures of 19S subunits, including proteasomal ATPases, ubiquitin receptors, deubiquitinating enzymes and subunits that contain PCI domain. This article is part of a Special Issue entitled The 26S Proteasome: When degradation is just not enough! (c) 2010 Elsevier B.V. All rights reserved.
Publisher
ELSEVIER SCIENCE BV
Issue Date
2011-02
Language
English
Article Type
Review
Keywords

19S REGULATORY PARTICLE; MESSENGER-RNA EXPORT; I-PRESENTED PEPTIDES; 20S PROTEASOME; DEUBIQUITINATING ENZYME; CRYSTAL-STRUCTURE; COP9 SIGNALOSOME; CORE PARTICLE; SACCHAROMYCES-CEREVISIAE; SUBUNIT INTERACTION

Citation

BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS, v.1809, no.2, pp.67 - 79

ISSN
1874-9399
DOI
10.1016/j.bbagrm.2010.08.008
URI
http://hdl.handle.net/10203/101468
Appears in Collection
MSE-Journal Papers(저널논문)
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