The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum–Derived Vesicles
The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum–Derived Vesicles
Members of the yeast p24 family, including Emp24p and Erv25p, form a heteromeric complex required for the efficient transport of selected proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The specific functions and sites of action of this complex are unknown. We show that Emp24p is directly required for efficient packaging of a lumenal cargo protein, Gas1p, into ER-derived vesicles. Emp24p and Erv25p can be directly cross-linked to Gas1p in ER-derived vesicles. Gap1p, which was not affected by emp24 mutation, was not cross-linked. These results suggest that the Emp24 complex acts as a cargo receptor in vesicle biogenesis from the ER.
- University of Basel Switzerland
- University of Seville Spain
Saccharomyces cerevisiae Proteins, Macromolecular Substances, protein sorting, Vesicular Transport Proteins, Golgi Apparatus, Endosomes, Saccharomyces cerevisiae, Endoplasmic Reticulum, Antibodies, Fungal Proteins, HSP70 Heat-Shock Proteins, COPII-coated vesicle, Membrane Glycoproteins, Sulfhydryl Reagents, Membrane Proteins, Biological Transport, Intracellular Membranes, Precipitin Tests, Cross-Linking Reagents, ER, Ethylmaleimide, Carrier Proteins, Protein Processing, Post-Translational, Erv25p
Saccharomyces cerevisiae Proteins, Macromolecular Substances, protein sorting, Vesicular Transport Proteins, Golgi Apparatus, Endosomes, Saccharomyces cerevisiae, Endoplasmic Reticulum, Antibodies, Fungal Proteins, HSP70 Heat-Shock Proteins, COPII-coated vesicle, Membrane Glycoproteins, Sulfhydryl Reagents, Membrane Proteins, Biological Transport, Intracellular Membranes, Precipitin Tests, Cross-Linking Reagents, ER, Ethylmaleimide, Carrier Proteins, Protein Processing, Post-Translational, Erv25p
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