The mammalian endoplasmic reticulum-associated degradation system.
The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic proteome and is accordingly endowed with specialized machinery to ensure that proteins deployed to the distal secretory pathway are correctly folded and assembled into native oligomeric complexes. Proteins...
| Príomhchruthaitheoirí: | , , |
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| Formáid: | Journal article |
| Teanga: | English |
| Foilsithe / Cruthaithe: |
2013
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| _version_ | 1826259473385127936 |
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| author | Olzmann, J Kopito, R Christianson, J |
| author_facet | Olzmann, J Kopito, R Christianson, J |
| author_sort | Olzmann, J |
| collection | OXFORD |
| description | The endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic proteome and is accordingly endowed with specialized machinery to ensure that proteins deployed to the distal secretory pathway are correctly folded and assembled into native oligomeric complexes. Proteins failing to meet this conformational standard are degraded by ER-associated degradation (ERAD), a complex process through which folding-defective proteins are selected and ultimately degraded by the ubiquitin-proteasome system. ERAD proceeds through four tightly coupled steps involving substrate selection, dislocation across the ER membrane, covalent conjugation with polyubiquitin, and proteasomal degradation. The ERAD machinery shows a modular organization with central ER membrane-embedded ubiquitin ligases linking components responsible for recognition in the ER lumen to the ubiquitin-proteasome system in the cytoplasm. The core ERAD machinery is highly conserved among eukaryotes and much of our basic understanding of ERAD organization has been derived from genetic and biochemical studies of yeast. In this article we discuss how the core ERAD machinery is organized in mammalian cells. |
| first_indexed | 2024-03-06T18:50:27Z |
| format | Journal article |
| id | oxford-uuid:10094d08-dc8c-4566-bd6a-ab89bbfe5d4b |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:50:27Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | oxford-uuid:10094d08-dc8c-4566-bd6a-ab89bbfe5d4b2022-03-26T09:54:20ZThe mammalian endoplasmic reticulum-associated degradation system.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:10094d08-dc8c-4566-bd6a-ab89bbfe5d4bEnglishSymplectic Elements at Oxford2013Olzmann, JKopito, RChristianson, JThe endoplasmic reticulum (ER) is the site of synthesis for nearly one-third of the eukaryotic proteome and is accordingly endowed with specialized machinery to ensure that proteins deployed to the distal secretory pathway are correctly folded and assembled into native oligomeric complexes. Proteins failing to meet this conformational standard are degraded by ER-associated degradation (ERAD), a complex process through which folding-defective proteins are selected and ultimately degraded by the ubiquitin-proteasome system. ERAD proceeds through four tightly coupled steps involving substrate selection, dislocation across the ER membrane, covalent conjugation with polyubiquitin, and proteasomal degradation. The ERAD machinery shows a modular organization with central ER membrane-embedded ubiquitin ligases linking components responsible for recognition in the ER lumen to the ubiquitin-proteasome system in the cytoplasm. The core ERAD machinery is highly conserved among eukaryotes and much of our basic understanding of ERAD organization has been derived from genetic and biochemical studies of yeast. In this article we discuss how the core ERAD machinery is organized in mammalian cells. |
| spellingShingle | Olzmann, J Kopito, R Christianson, J The mammalian endoplasmic reticulum-associated degradation system. |
| title | The mammalian endoplasmic reticulum-associated degradation system. |
| title_full | The mammalian endoplasmic reticulum-associated degradation system. |
| title_fullStr | The mammalian endoplasmic reticulum-associated degradation system. |
| title_full_unstemmed | The mammalian endoplasmic reticulum-associated degradation system. |
| title_short | The mammalian endoplasmic reticulum-associated degradation system. |
| title_sort | mammalian endoplasmic reticulum associated degradation system |
| work_keys_str_mv | AT olzmannj themammalianendoplasmicreticulumassociateddegradationsystem AT kopitor themammalianendoplasmicreticulumassociateddegradationsystem AT christiansonj themammalianendoplasmicreticulumassociateddegradationsystem AT olzmannj mammalianendoplasmicreticulumassociateddegradationsystem AT kopitor mammalianendoplasmicreticulumassociateddegradationsystem AT christiansonj mammalianendoplasmicreticulumassociateddegradationsystem |