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The yeast p24 complex regulates gpi-anchored protein Transport and quality control by monitoring anchor remodeling

Opened Access The yeast p24 complex regulates gpi-anchored protein Transport and quality control by monitoring anchor remodeling

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Autor: Castillon, Guillaume Alain
Aguilera Romero, María Auxiliadora
Manzano-López, Javier
Epstein, Sharon
Kajiwara, Kentaro
Funato, Kouichi
Watanabe, Reika
Riezman, Howard
Muñiz Guinea, Manuel
Departamento: Universidad de Sevilla. Departamento de Biología Celular
Fecha: 2011
Publicado en: Molecular Biology of the Cell, 22 (16), 2924-2936
Tipo de documento: Artículo
Resumen: 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 traffick - ing. 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 incorpo - ration 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 intracellu...
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Tamaño: 2.067Mb
Formato: PDF

URI: http://hdl.handle.net/11441/40101

DOI: 10.1091/mbc.E11-04-0294

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