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The eukaryotic endoplasmic reticulum (ER) maintains protein homeostasis by eliminating unwanted proteins through the evolutionarily conserved ER-associated degradation (ERAD) pathway. During ERAD, maturation-defective and surplus polypeptides are evicted from the ER lumen and/or lipid bilayer through the process of retrotranslocation and ultimately degraded by the proteasome. An integral facet of the ERAD mechanism is the ubiquitin system, composed of the ubiquitin modifier and the factors for assembling, processing and binding ubiquitin chains on conjugated substrates. Beyond simply marking polypeptides for degradation, the ubiquitin system is functionally intertwined with retrotranslocation machinery to transport polypeptides across the ER membrane.

Original publication

DOI

10.1038/nsmb.2793

Type

Journal article

Journal

Nature structural & molecular biology

Publication Date

04/2014

Volume

21

Pages

325 - 335

Addresses

1] Ludwig Institute for Cancer Research, University of Oxford, Oxford, UK. [2].

Keywords

Endoplasmic Reticulum, Animals, Proteasome Endopeptidase Complex, Proteins, Ubiquitins, Ubiquitin, Protein Folding, Homeostasis, Models, Biological, Proteolysis, Ubiquitin-Specific Proteases