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ER-Associated Degradation of Membrane Proteins in Yeast

Proteins destined for the secretory pathway are translocated into the endoplasmic reticulum (ER), where they are subjected to a variety of post-translational modifications before they reach their final destination. Newly synthesized proteins that have defect in polypeptide folding or subunit assembl...

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Detalles Bibliográficos
Autores principales: Pety de Thozée, Cédric, Ghislain, Michel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: TheScientificWorldJOURNAL 2006
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5917121/
https://www.ncbi.nlm.nih.gov/pubmed/16921443
http://dx.doi.org/10.1100/tsw.2006.191
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author Pety de Thozée, Cédric
Ghislain, Michel
author_facet Pety de Thozée, Cédric
Ghislain, Michel
author_sort Pety de Thozée, Cédric
collection PubMed
description Proteins destined for the secretory pathway are translocated into the endoplasmic reticulum (ER), where they are subjected to a variety of post-translational modifications before they reach their final destination. Newly synthesized proteins that have defect in polypeptide folding or subunit assembly are recognized by quality control systems and eliminated by the 26S proteasome, a cytosolic ATP-dependent proteolytic machinery. Delivery of non-native ER proteins to the proteasome requires retrograde transport across the ER membrane and depends on a protein-unfolding machine consisting of Cdc48p, Ufd1p, and Npl4p. Recent studies in yeast have highlighted the possible function of the Sar1p/COPII machinery in ER-associated degradation of some lumenal and membrane proteins.
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spelling pubmed-59171212018-06-03 ER-Associated Degradation of Membrane Proteins in Yeast Pety de Thozée, Cédric Ghislain, Michel ScientificWorldJournal Review Article Proteins destined for the secretory pathway are translocated into the endoplasmic reticulum (ER), where they are subjected to a variety of post-translational modifications before they reach their final destination. Newly synthesized proteins that have defect in polypeptide folding or subunit assembly are recognized by quality control systems and eliminated by the 26S proteasome, a cytosolic ATP-dependent proteolytic machinery. Delivery of non-native ER proteins to the proteasome requires retrograde transport across the ER membrane and depends on a protein-unfolding machine consisting of Cdc48p, Ufd1p, and Npl4p. Recent studies in yeast have highlighted the possible function of the Sar1p/COPII machinery in ER-associated degradation of some lumenal and membrane proteins. TheScientificWorldJOURNAL 2006-08-17 /pmc/articles/PMC5917121/ /pubmed/16921443 http://dx.doi.org/10.1100/tsw.2006.191 Text en Copyright © 2006 Cédric Pety de Thozée and Michel Ghislain. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review Article
Pety de Thozée, Cédric
Ghislain, Michel
ER-Associated Degradation of Membrane Proteins in Yeast
title ER-Associated Degradation of Membrane Proteins in Yeast
title_full ER-Associated Degradation of Membrane Proteins in Yeast
title_fullStr ER-Associated Degradation of Membrane Proteins in Yeast
title_full_unstemmed ER-Associated Degradation of Membrane Proteins in Yeast
title_short ER-Associated Degradation of Membrane Proteins in Yeast
title_sort er-associated degradation of membrane proteins in yeast
topic Review Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5917121/
https://www.ncbi.nlm.nih.gov/pubmed/16921443
http://dx.doi.org/10.1100/tsw.2006.191
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