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The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis

Voges, D., Zwickl, P., Baumeister, W.·1999·Annual Review of Biochemistry

Abstract

▪ Abstract In eukaryotic cells, most proteins in the cytosol and nucleus are degraded via the ubiquitin-proteasome pathway. The 26S proteasome is a 2.5-MDa molecular machine built from ∼31 different subunits, which catalyzes protein degradation. It contains a barrel-shaped proteolytic core complex (the 20S proteasome), capped at one or both ends by 19S regulatory complexes, which recognize ubiquitinated proteins. The regulatory complexes are also implicated in unfolding and translocation of ubiquitinated targets into the interior of the 20S complex, where they are degraded to oligopeptides. Structure, assembly and enzymatic mechanism of the 20S complex have been elucidated, but the functional organization of the 19S complex is less well understood. Most subunits of the 19S complex have been identified, however, specific functions have been assigned to only a few. A low-resolution structure of the 26S proteasome has been obtained by electron microscopy, but the precise arrangement of subunits in the 19S complex is unclear.

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Crossref · 10.1146/annurev.biochem.68.1.1015

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  • Chains linked via K48 in ubiquitin typically lead to degradation of the substrate by the proteasome.

    “Chains linked via Lys48 (K48) in Ub, the best-characterized type of Ub conjugation, typically lead to degradation of the substrate by the proteasome (Voges et al, 1999).”

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Metadata

Authors
Voges, D., Zwickl, P., & Baumeister, W.
Venue
Annual Review of Biochemistry
Published
1999-06
Volume
68
Issue
1
Pages
1015-1068
ISSN
  • 0066-4154
  • 1545-4509
Cited by
1,608
References
3
Language
en

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