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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| Main Authors: | , |
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| Format: | Article |
| Language: | English |
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Wiley
2006-01-01
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| Series: | The Scientific World Journal |
| Online Access: | http://dx.doi.org/10.1100/tsw.2006.191 |
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| _version_ | 1850160108909101056 |
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| author | Cédric Pety de Thozée Michel Ghislain |
| author_facet | Cédric Pety de Thozée Michel Ghislain |
| author_sort | Cédric Pety de Thozée |
| collection | DOAJ |
| 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. |
| format | Article |
| id | doaj-art-b0f4e95c04934fbda969ef59b75a5881 |
| institution | OA Journals |
| issn | 1537-744X |
| language | English |
| publishDate | 2006-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | The Scientific World Journal |
| spelling | doaj-art-b0f4e95c04934fbda969ef59b75a58812025-08-20T02:23:15ZengWileyThe Scientific World Journal1537-744X2006-01-01696798310.1100/tsw.2006.191ER-Associated Degradation of Membrane Proteins in YeastCédric Pety de Thozée0Michel Ghislain1Unité Biochimie Physiologique Institut des Sciences de la Vie Université Catholique de Louvain, B-1348 Louvain-la-Neuve, BelgiumUnité Biochimie Physiologique Institut des Sciences de la Vie Université Catholique de Louvain, B-1348 Louvain-la-Neuve, BelgiumProteins 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.http://dx.doi.org/10.1100/tsw.2006.191 |
| spellingShingle | Cédric Pety de Thozée Michel Ghislain ER-Associated Degradation of Membrane Proteins in Yeast The Scientific World Journal |
| 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 |
| url | http://dx.doi.org/10.1100/tsw.2006.191 |
| work_keys_str_mv | AT cedricpetydethozee erassociateddegradationofmembraneproteinsinyeast AT michelghislain erassociateddegradationofmembraneproteinsinyeast |