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J Biol Chem, Vol. 274, Issue 7, 4389-4399, February 12, 1999
From the Departments of Cell and Molecular Biology, The Scripps
Research Institute, La Jolla, California 92037
The COPII coat complex found on endoplasmic
reticulum (ER)-derived vesicles plays a critical role in cargo
selection. We now address the potential role of biosynthetic cargo in
modulating COPII coat assembly and vesicle budding. The ER accumulation
of vesicular stomatitis glycoprotein (VSV-G), a transmembrane protein, or the soluble PiZ variant of 
1-antitrypsin, reduced levels of general COPII vesicle formation in vivo. Consistent with
this result, conditions that prevent the export of VSV-G from the ER led to a significant inhibition of general COPII vesicle budding from
ER microsomes and the export of an endogenous recycling protein p58
in vitro. In contrast, synchronized export of VSV-G
stimulated COPII vesicle budding both in vivo and in
vitro. Under conditions where VSV-G is retained in the ER, we
find that it can to be recovered in pre-budding complexes containing
COPII components. These results suggest that the export of biosynthetic
cargo is integrated with ER functions involved in protein folding and
oligomerization. The ability of biosynthetic cargo to prevent or
enhance ER export suggests that interactions of cargo with the COPII
machinery contribute to the formation of vesicles budding from the ER.
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