Now showing items 1-5 of 5
The yeast p24 complex is required for the formation of COPI retrograde transport vesicles from the Golgi apparatus [Article]
(Rockefeller University Press, 2008)
The p24 family members are transmembrane proteins assembled into heteromeric complexes that continuously cycle between the ER and the Golgi apparatus. These cargo proteins were assumed to play a structural role in COPI ...
The yeast p24 complex regulates gpi-anchored protein Transport and quality control by monitoring anchor remodeling [Article]
(American Society for Cell Biology, 2011)
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 ...
The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles [Article]
(Rockefeller University Press, 2000)
Members of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex re- quired for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the Golgi ap- paratus. The ...
Osh proteins regulate COPII-mediated vesicular transport of ceramide from the endoplasmic reticulum in budding yeast [Article]
(Company of Biologists Ltd, 2014)
Lipids synthesized at the endoplasmic reticulum (ER) are delivered to the Golgi by vesicular and non-vesicular pathways. ER-to-Golgi transport is crucial for maintaining the different membrane lipid composition and identities ...
Limited ER quality control for GPI-anchored proteins [Article]
(Rockefeller University Press, 2016)
Endoplasmic reticulum (ER) quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD). Misfolded glycophosphatidylinositol-anchored proteins (GPI-APs) are, however, generally poor ...