The Emp24 Complex Recruits a Specific Cargo Molecule into Endoplasmic Reticulum-derived Vesicles

doi:10.1083/jcb.148.5.925

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© The Rockefeller University Press, 0021-9525/2000/3/925/ $5.00
The Journal of Cell Biology, Volume 148, Number 5, March 6, 2000 925-930

Original Article

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

Manuel Muñiz^a, Claude Nuoffer^a, Hans-Peter Hauri^a, and Howard Riezman^a
^a Biozentrum of the University of Basel, CH-4056 Basel, Switzerland

Correspondence to: Howard Riezman, Biozentrum of the University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. Tel:41-61-267-2160 Fax:41-61-267-2149 E-mail:howard.riezman{at}unibas.ch.

Members of the yeast p24 family, including Emp24p and Erv25p,form a heteromeric complex required for the efficient transportof selected proteins from the endoplasmic reticulum (ER) tothe Golgi apparatus. The specific functions and sites of actionof this complex are unknown. We show that Emp24p is directlyrequired for efficient packaging of a lumenal cargo protein,Gas1p, into ER-derived vesicles. Emp24p and Erv25p can be directlycross-linked to Gas1p in ER-derived vesicles. Gap1p, which wasnot affected by emp24 mutation, was not cross-linked. Theseresults suggest that the Emp24 complex acts as a cargo receptorin vesicle biogenesis from the ER.

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

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