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Vol. 9, Issue 6, 1265-1278, June 1998
*Department of Cell Biology and Anatomy, University of Alberta,
Edmonton, Alberta, Canada T6G 2H7; and
Rubella virus E1 glycoprotein normally complexes with E2 in the
endoplasmic reticulum (ER) to form a heterodimer that is transported to
and retained in the Golgi complex. In a previous study, we showed that
in the absence of E2, unassembled E1 subunits accumulate in a tubular
pre-Golgi compartment whose morphology and biochemical properties are
distinct from both rough ER and Golgi. We hypothesized that this
compartment corresponds to hypertrophied ER exit sites that have
expanded in response to overexpression of E1. In the present study we
constructed BHK cells stably expressing E1 protein containing a
cytoplasmically disposed epitope and isolated the pre-Golgi compartment
from these cells by cell fractionation and immunoisolation. Double
label indirect immunofluorescence in cells and
immunoblotting of immunoisolated tubular networks
revealed that proteins involved in formation of ER-derived transport
vesicles, namely p58/ERGIC 53, Sec23p, and Sec13p, were concentrated in the E1-containing pre-Golgi compartment. Furthermore, budding structures were evident in these membrane profiles, and a highly abundant but unknown 65-kDa protein was also present. By comparison, marker proteins of the rough ER, Golgi, and COPI vesicles were not
enriched in these membranes. These results demonstrate that the
composition of the tubular networks corresponds to that expected of ER
exit sites. Accordingly, we propose the name SEREC (smooth ER exit
compartment) for this structure.
Division of
Cellular and Molecular Medicine, University of California, San Diego,
La Jolla, California 92093
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