Journal
FEBS LETTERS
Volume 582, Issue 30, Pages 4143-4146Publisher
WILEY
DOI: 10.1016/j.febslet.2008.11.015
Keywords
Protein quality control; Misfolded protein; Ubiquitin ligase; Ubr1; Proteasome; Protein degradation
Funding
- Deutsche Forschungsgemeinschaft, Bonn
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Protein quality control and subsequent elimination of terminally misfolded proteins occurs via theubiquitin-proteasome system. Tagging of misfolded proteins with ubiquitin for degradation depends on a cascade of reactions involving an ubiquitin activating enzyme (E1), ubiquitin conjugating enzymes (E2) and ubiquitin ligases (E3). While ubiquitin ligases responsible for targeting misfolded secretory proteins to proteasomal degradation (ERAD) have been uncovered, no such E3 enzymes have been found for elimination of misfolded cytoplasmic proteins in yeast. Here we report on the discovery of Ubr1, the E3 ligase of the N-end rule pathway, to be responsible for targeting misfolded cytosoplasmic protein to proteasomal degradation. (c) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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