Degradation of damaged proteins: The main function of the 20S proteasome

Andrew M. Pickering, Kelvin J.A. Davies

Research output: Chapter in Book/Report/Conference proceedingChapter

96 Scopus citations

Abstract

Cellular proteins are exposed to oxidative modification and other forms of damage through oxidative stress and disease, and as a consequence of aging. This oxidative damage results in loss and/or modification of protein function, which in turn compromises cell function and may even cause cell death. Therefore, the removal of damaged proteins is extremely important for the maintenance of normal cell function. The 20S proteasome functions primarily as a system for removal of such damaged proteins. Unlike the 26S proteasome, the 20S proteasome exhibits a high degree of selectivity in degrading the oxidized, or otherwise damaged, forms of cell proteins. The 20S proteasome is broadly distributed throughout the cell and has a range of specific functions in different organelles, which are controlled through a number of proteasome regulators. It is also activated, and its synthesis is induced, under conditions of enhanced oxidative stress, thus permitting greater removal of damaged proteins.

Original languageEnglish (US)
Title of host publicationProgress in Molecular Biology and Translational Science
PublisherElsevier B.V.
Pages227-248
Number of pages22
DOIs
StatePublished - 2012

Publication series

NameProgress in Molecular Biology and Translational Science
Volume109
ISSN (Print)1877-1173

Keywords

  • 11S
  • 20S proteasome
  • 26S proteasome
  • Free radicals
  • HSP70
  • Hydrogen peroxide
  • Oxidative stress
  • PARP
  • Pa200
  • Pa28αβ

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology

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