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© The Rockefeller University Press, 0021-9525/2000//925 $5.00
The Journal of Cell Biology, Volume 148, Number 5, , 2000 925-930

Original Article

The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum–Derived Vesicles



Manuel Muñiza, Claude Nuoffera, Hans-Peter Hauria, and Howard Riezmana

a Biozentrum of the University of Basel, CH-4056 Basel, Switzerland
Biozentrum of the University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.41-61-267-214941-61-267-2160

howard.riezman{at}unibas.ch

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.

Key Words: COPII-coated vesicles • ER • Erv25p • Saccharomyces cerevisiae • protein sorting

© 2000 The Rockefeller University Press

Abbreviations used in this paper: DSG, disuccinimidyl glutarate; DSP, dithiobis(succinimidylpropionate); gp{alpha}F, glycosylated pro {alpha} factor; GPI, glycosylphosphatidylinositol.


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