Structure characterization of the 26S proteasome

Biochim Biophys Acta. 2011 Feb;1809(2):67-79. doi: 10.1016/j.bbagrm.2010.08.008. Epub 2010 Aug 26.

Abstract

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!

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Models, Molecular
  • Proteasome Endopeptidase Complex / chemistry*
  • Protein Processing, Post-Translational
  • Protein Structure, Secondary
  • Protein Subunits / chemistry

Substances

  • Protein Subunits
  • Proteasome Endopeptidase Complex
  • ATP dependent 26S protease