1 research outputs found
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 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
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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
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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 remodelin