Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Castillon, Guillaume A., Aguilera-Romero, Auxiliadora, Manzano-Lopez, Javier, Epstein, Sharon, Kajiwara, Kentaro, Funato, Kouichi, Watanabe, Reika, Riezman, Howard, Muñiz, Manuel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
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
_version_ 1782210048183762944
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
work_keys_str_mv AT castillonguillaumea theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT aguileraromeroauxiliadora theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT manzanolopezjavier theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT epsteinsharon theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT kajiwarakentaro theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT funatokouichi theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT watanabereika theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT riezmanhoward theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT munizmanuel theyeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT castillonguillaumea yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT aguileraromeroauxiliadora yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT manzanolopezjavier yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT epsteinsharon yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT kajiwarakentaro yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT funatokouichi yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT watanabereika yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT riezmanhoward yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling
AT munizmanuel yeastp24complexregulatesgpianchoredproteintransportandqualitycontrolbymonitoringanchorremodeling