Protein quality control in the ER: balancing the ubiquitin checkbook

Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss th...

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Published in	Trends in cell biology Vol. 22; no. 1; pp. 22 - 32
Main Authors	Claessen, Jasper H.L., Kundrat, Lenka, Ploegh, Hidde L.
Format	Journal Article
Language	English
Published	England Elsevier Ltd 01.01.2012
Subjects	Animals endoplasmic reticulum Endoplasmic Reticulum - metabolism Humans Pathology polypeptides proteasome endopeptidase complex Protein Binding Protein Folding Protein Processing, Post-Translational proteolysis quality control Substrate Specificity ubiquitin Ubiquitin - metabolism ubiquitin-protein ligase
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ISSN	0962-8924 1879-3088 1879-3088
DOI	10.1016/j.tcb.2011.09.010

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Abstract	Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ligase complexes as gatekeepers for membrane passage. We then examine the type of ubiquitin modification applied to the misfolded ER protein and the role of de-ubiquitylating enzymes in the extraction of proteins from the ER.
AbstractList	Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ligase complexes as gatekeepers for membrane passage. We then examine the type of ubiquitin modification applied to the misfolded ER protein and the role of de-ubiquitylating enzymes in the extraction of proteins from the ER. Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. Here, we discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ligase complexes as gatekeepers for membrane passage. We then examine the type of ubiquitin modification applied to the misfolded ER protein and the role of de-ubiquitylating enzymes in the extraction of proteins from the ER. Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ligase complexes as gatekeepers for membrane passage. We then examine the type of ubiquitin modification applied to the misfolded ER protein and the role of de-ubiquitylating enzymes in the extraction of proteins from the ER.Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the cytoplasm and targeted for destruction by the proteasome. Ubiquitin conjugation is essential for both extraction and proteolysis. We discuss the role of the ubiquitin conjugation machinery in this pathway and focus on the role of ubiquitin ligase complexes as gatekeepers for membrane passage. We then examine the type of ubiquitin modification applied to the misfolded ER protein and the role of de-ubiquitylating enzymes in the extraction of proteins from the ER.
Author	Ploegh, Hidde L. Claessen, Jasper H.L. Kundrat, Lenka
Author_xml	– sequence: 1 givenname: Jasper H.L. surname: Claessen fullname: Claessen, Jasper H.L. – sequence: 2 givenname: Lenka surname: Kundrat fullname: Kundrat, Lenka – sequence: 3 givenname: Hidde L. surname: Ploegh fullname: Ploegh, Hidde L. email: ploegh@wi.mit.edu
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/22055166$$D View this record in MEDLINE/PubMed
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Snippet	Protein maturation in the endoplasmic reticulum (ER) is subject to stringent quality control. Terminally misfolded polypeptides are usually ejected into the...
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SubjectTerms	Animals endoplasmic reticulum Endoplasmic Reticulum - metabolism Humans Pathology polypeptides proteasome endopeptidase complex Protein Binding Protein Folding Protein Processing, Post-Translational proteolysis quality control Substrate Specificity ubiquitin Ubiquitin - metabolism ubiquitin-protein ligase
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Title	Protein quality control in the ER: balancing the ubiquitin checkbook
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