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J. Biol. Chem., Vol. 275, Issue 23, 17718-17727, June 9, 2000
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From the Department of Biochemistry and Cell Biology, Institute for
Cell and Developmental Biology, State University of New York, Stony
Brook, New York 11794-5215
The substrates for glycan synthesis in the lumen
of the Golgi are nucleotide sugars that must be transported from the
cytosol by specific membrane-bound transporters. The principal
nucleotide sugar used for glycosylation in the Golgi of the yeast
Saccharomyces cerevisiae is GDP-mannose, whose lumenal
transport is mediated by the VRG4 gene product. As the sole
provider of lumenal mannose, the Vrg4 protein functions as a key
regulator of glycosylation in the yeast Golgi. We have undertaken a
functional analysis of Vrg4p as a model for understanding nucleotide
sugar transport in the Golgi. Here, we analyzed epitope-tagged alleles
of VRG4. Gel filtration chromatography and
co-immunoprecipitation experiments demonstrate that the Vrg4 protein
forms homodimers with specificity and high affinity. Deletion analyses
identified two regions essential for Vrg4p function. Mutant Vrg4
proteins lacking the predicted C-terminal membrane-spanning domain fail
to assemble into oligomers (Abe, M., Hashimoto, H., and Yoda, K. (1999)
FEBS Lett. 458, 309-312) and are unstable, while proteins
lacking the N-terminal cytosolic tail are stable and
multimerize efficiently, but are mislocalized to the endoplasmic
reticulum (ER). Fusion of the N terminus of Vrg4p to related ER
membrane proteins promote their transport to the Golgi, suggesting that
sequences in the N terminus supply information for ER export. The
dominant negative phenotype resulting from overexpression of truncated
Vrg4-
Distinct Protein Domains of the Yeast Golgi GDP-mannose
Transporter Mediate Oligomer Assembly and Export from the
Endoplasmic Reticulum*
N proteins provides strong genetic evidence for
homodimer formation in vivo. These studies are consistent
with a model in which Vrg4p oligomerizes in the ER and is subsequently
transported to the Golgi via a mechanism that involves positive sorting
rather than passive default.
*
This work was supported by Grant GM48467 from the National
Institutes of Health (to N. D.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 631-632-9309;
Fax: 631-632-8575; E-mail: ndean@notes.cc.sunysb.edu.
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