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Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast
Misfolded and/or unassembled secretory and membrane proteins in the endoplasmic reticulum (ER) may be retro-translocated into the cytoplasm, where they undergo ER-associated degradation, or ERAD. The mechanisms by which misfolded proteins are recognized and degraded through this pathway have been st...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2021
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7865462/ https://www.ncbi.nlm.nih.gov/pubmed/33494405 http://dx.doi.org/10.3390/ijms22031061 |
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author | Nakatsukasa, Kunio |
author_facet | Nakatsukasa, Kunio |
author_sort | Nakatsukasa, Kunio |
collection | PubMed |
description | Misfolded and/or unassembled secretory and membrane proteins in the endoplasmic reticulum (ER) may be retro-translocated into the cytoplasm, where they undergo ER-associated degradation, or ERAD. The mechanisms by which misfolded proteins are recognized and degraded through this pathway have been studied extensively; however, our understanding of the physiological role of ERAD remains limited. This review describes the biosynthesis and quality control of glycosylphosphatidylinositol (GPI)-anchored proteins and briefly summarizes the relevance of ERAD to these processes. While recent studies suggest that ERAD functions as a fail-safe mechanism for the degradation of misfolded GPI-anchored proteins, several pieces of evidence suggest an intimate interaction between ERAD and the biosynthesis of GPI-anchored proteins. |
format | Online Article Text |
id | pubmed-7865462 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-78654622021-02-07 Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast Nakatsukasa, Kunio Int J Mol Sci Review Misfolded and/or unassembled secretory and membrane proteins in the endoplasmic reticulum (ER) may be retro-translocated into the cytoplasm, where they undergo ER-associated degradation, or ERAD. The mechanisms by which misfolded proteins are recognized and degraded through this pathway have been studied extensively; however, our understanding of the physiological role of ERAD remains limited. This review describes the biosynthesis and quality control of glycosylphosphatidylinositol (GPI)-anchored proteins and briefly summarizes the relevance of ERAD to these processes. While recent studies suggest that ERAD functions as a fail-safe mechanism for the degradation of misfolded GPI-anchored proteins, several pieces of evidence suggest an intimate interaction between ERAD and the biosynthesis of GPI-anchored proteins. MDPI 2021-01-21 /pmc/articles/PMC7865462/ /pubmed/33494405 http://dx.doi.org/10.3390/ijms22031061 Text en © 2021 by the author. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Review Nakatsukasa, Kunio Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast |
title | Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast |
title_full | Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast |
title_fullStr | Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast |
title_full_unstemmed | Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast |
title_short | Potential Physiological Relevance of ERAD to the Biosynthesis of GPI-Anchored Proteins in Yeast |
title_sort | potential physiological relevance of erad to the biosynthesis of gpi-anchored proteins in yeast |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7865462/ https://www.ncbi.nlm.nih.gov/pubmed/33494405 http://dx.doi.org/10.3390/ijms22031061 |
work_keys_str_mv | AT nakatsukasakunio potentialphysiologicalrelevanceoferadtothebiosynthesisofgpianchoredproteinsinyeast |