COPII–cargo interactions direct protein sorting into ER-derived transport vesicles

Meta J. Kuehn, Johannes M. Herrmann and Randy Schekman ()
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Meta J. Kuehn: Barker Hall, Howard Hughes Medical Institute, University of California
Johannes M. Herrmann: Barker Hall, Howard Hughes Medical Institute, University of California
Randy Schekman: Barker Hall, Howard Hughes Medical Institute, University of California

Nature, 1998, vol. 391, issue 6663, 187-190

Abstract: Abstract Vesicles coated with coat protein complex II (COPII) selectively transport molecules (cargo) and vesicle fusion proteins from the endoplasmic reticulum (ER) to the Golgi complex1,2,3. We have investigated the role of coat proteins in cargo selection and recruitment. We isolated integral membrane and soluble cargo proteins destined for transport from the ER in complexes formed in the presence of Sar1 and Sec23/24, a subset of the COPII components, and GTP or GMP-PNP. Vesicle fusion proteins of the vSNARE family and Emp24, a member of a putative cargo carrier family4, were also found in COPII complexes. The inclusion of amino-acid permease molecules into the complex depended on the presence of Shr3, a protein required for the permease to leave the ER3,5. Resident ER proteins Sec61, BiP (Kar2) and Shr3 were not included in the complexes, indicating that the COPII components bound specifically to vesicle cargo. COPII–cargo complexes and putative cargo adaptor–cargo complexes were also isolated from COPII vesicles. Our results indicate that cargo packaging signals and soluble cargo adaptors are recognized by a recruitment complex comprising Sar1–GTP and Sec23/24.

Date: 1998
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DOI: 10.1038/34438

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