title: The yeast p24 complex regulates GPI-anchored protein transport and quality control by monitoring anchor remodeling.
abstract: 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.
authors.affiliation: Department of Biochemistry, Sciences II, University of Geneva, CH-1211 Geneva 4, Switzerland.
authors.forename: Guillaume A
authors.initials: GA
authors.lastname: Castillon
authors.forename: Auxiliadora
authors.initials: A
authors.lastname: Aguilera-Romero
authors.forename: Javier
authors.initials: J
authors.lastname: Manzano-Lopez
authors.forename: Sharon
authors.initials: S
authors.lastname: Epstein
authors.forename: Kentaro
authors.initials: K
authors.lastname: Kajiwara
authors.forename: Kouichi
authors.initials: K
authors.lastname: Funato
authors.forename: Reika
authors.initials: R
authors.lastname: Watanabe
authors.forename: Howard
authors.initials: H
authors.lastname: Riezman
authors.forename: Manuel
authors.initials: M
authors.lastname: Muñiz
mesh_terms: D001665:Binding Sites; D004721:Endoplasmic Reticulum / Q000378:metabolism; D059865:Endoplasmic Reticulum Stress; D058851:GPI-Linked Proteins / Q000378:metabolism*; D055786:Gene Knockout Techniques; D017261:Glycosylphosphatidylinositols / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism; D008565:Membrane Proteins / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D021381:Protein Transport; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D056811:Unfolded Protein Response; D033921:Vesicular Transport Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
chemical_list: D058851:GPI-Linked Proteins; D017261:Glycosylphosphatidylinositols; D008565:Membrane Proteins; D046912:Multiprotein Complexes; C120079:SFB3 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D033921:Vesicular Transport Proteins