Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 21, Issue 4, Pages 325-335Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2793
Keywords
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Funding
- NIDDK
- US National Institutes of Health
- J.C.C
- Cancer Research and the UK Medical Research Council
- MRC [MR/L001209/1] Funding Source: UKRI
- Medical Research Council [MR/L001209/1] Funding Source: researchfish
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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.
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