Artículo
The yeast p24 complex regulates gpi-anchored protein Transport and quality control by monitoring anchor remodeling
Autor/es | Castillon, Guillaume Alain
Aguilera Romero, María Auxiliadora Manzano López, Javier Epsteina, Sharon Kajiwarac, Kentaro Funato, Kouichi Watanabe, Reika Riezman, Howard Muñiz Guinea, Manuel |
Departamento | Universidad de Sevilla. Departamento de Biología Celular |
Fecha de publicación | 2011 |
Fecha de depósito | 2016-04-19 |
Publicado en |
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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 ... 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 intracellular transport and coordinates this with correct anchor remodeling |
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