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The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling
Glycosylphosphatidylinositol (GPI)-anchored proteins are secretory proteins that are attached to the cell surface of eukaryotic cells by a glycolipid moiety. Once GPI anchoring has occurred in the lumen of the endoplasmic reticulum (ER), the structure of the lipid part on the GPI anchor undergoes a...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3154887/ https://www.ncbi.nlm.nih.gov/pubmed/21680708 http://dx.doi.org/10.1091/mbc.E11-04-0294 |
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author | Castillon, Guillaume A. Aguilera-Romero, Auxiliadora Manzano-Lopez, Javier Epstein, Sharon Kajiwara, Kentaro Funato, Kouichi Watanabe, Reika Riezman, Howard Muñiz, Manuel |
author_facet | Castillon, Guillaume A. Aguilera-Romero, Auxiliadora Manzano-Lopez, Javier Epstein, Sharon Kajiwara, Kentaro Funato, Kouichi Watanabe, Reika Riezman, Howard Muñiz, Manuel |
author_sort | Castillon, Guillaume A. |
collection | PubMed |
description | Glycosylphosphatidylinositol (GPI)-anchored proteins are secretory proteins that are attached to the cell surface of eukaryotic cells by a glycolipid moiety. Once GPI anchoring has occurred in the lumen of the endoplasmic reticulum (ER), the structure of the lipid part on the GPI anchor undergoes a remodeling process prior to ER exit. In this study, we provide evidence suggesting that the yeast p24 complex, through binding specifically to GPI-anchored proteins in an anchor-dependent manner, plays a dual role in their selective trafficking. First, the p24 complex promotes efficient ER exit of remodeled GPI-anchored proteins after concentration by connecting them with the COPII coat and thus facilitates their incorporation into vesicles. Second, it retrieves escaped, unremodeled GPI-anchored proteins from the Golgi to the ER in COPI vesicles. Therefore the p24 complex, by sensing the status of the GPI anchor, regulates GPI-anchored protein intracellular transport and coordinates this with correct anchor remodeling. |
format | Online Article Text |
id | pubmed-3154887 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-31548872011-10-30 The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling Castillon, Guillaume A. Aguilera-Romero, Auxiliadora Manzano-Lopez, Javier Epstein, Sharon Kajiwara, Kentaro Funato, Kouichi Watanabe, Reika Riezman, Howard Muñiz, Manuel Mol Biol Cell Articles Glycosylphosphatidylinositol (GPI)-anchored proteins are secretory proteins that are attached to the cell surface of eukaryotic cells by a glycolipid moiety. Once GPI anchoring has occurred in the lumen of the endoplasmic reticulum (ER), the structure of the lipid part on the GPI anchor undergoes a remodeling process prior to ER exit. In this study, we provide evidence suggesting that the yeast p24 complex, through binding specifically to GPI-anchored proteins in an anchor-dependent manner, plays a dual role in their selective trafficking. First, the p24 complex promotes efficient ER exit of remodeled GPI-anchored proteins after concentration by connecting them with the COPII coat and thus facilitates their incorporation into vesicles. Second, it retrieves escaped, unremodeled GPI-anchored proteins from the Golgi to the ER in COPI vesicles. Therefore the p24 complex, by sensing the status of the GPI anchor, regulates GPI-anchored protein intracellular transport and coordinates this with correct anchor remodeling. The American Society for Cell Biology 2011-08-15 /pmc/articles/PMC3154887/ /pubmed/21680708 http://dx.doi.org/10.1091/mbc.E11-04-0294 Text en © 2011 Castillon et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology. |
spellingShingle | Articles Castillon, Guillaume A. Aguilera-Romero, Auxiliadora Manzano-Lopez, Javier Epstein, Sharon Kajiwara, Kentaro Funato, Kouichi Watanabe, Reika Riezman, Howard Muñiz, Manuel The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling |
title | The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling |
title_full | The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling |
title_fullStr | The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling |
title_full_unstemmed | The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling |
title_short | The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling |
title_sort | yeast p24 complex regulates gpi-anchored protein transport and quality control by monitoring anchor remodeling |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3154887/ https://www.ncbi.nlm.nih.gov/pubmed/21680708 http://dx.doi.org/10.1091/mbc.E11-04-0294 |
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