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A more recent version of this article appeared on August 1, 2003
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Submitted on March 5, 2003
Accepted on April 11, 2003
1 Dept. of Cell Biology and Histology, AMC, University of Amsterdam, PO box 22700, 1100 DE Amsterdam, The Netherlands; Dept. of Cell Biology, University Medical Center G02.525, Institute of Biomembranes, 3584 CX Utrecht, The Netherlands; and Max-Planck-Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany
2 Dept. of Cell Biology and Histology, AMC, University of Amsterdam, PO box 22700, 1100 DE Amsterdam, The Netherlands; Dept. of Membrane Enzymology, CBLE, Institute of Biomembranes, Padualaan 8, 3584 CH Utrecht, The Netherlands
3 Cell Biology and Biophysics Programme, European Molecular Biology Laboratory, Postfach 10.22.09, 69012 Heidelberg, Germany
4 Dept. of Physiological Chemistry, Tokyo Metropolitan Institute of Medical Science (Rinshoken), 18-22 Honkomagome 3-chome, Bunkyo-ku, Tokyo 113-8613, Japan
5 Dept. of Cell Biology, University Medical Center G02.525, Institute of Biomembranes, 3584 CX Utrecht, The Netherlands
* Corresponding author. E-mail address: g.vanmeer{at}chem.uu.nl.
UDP-galactose reaches the Golgi lumen through the UDP-galactose transporter (UGT) and is used for the galactosylation of proteins and lipids. Ceramides are galactosylated within the endoplasmic reticulum by the UDP-galactose:ceramidegalactosyltransferase. It is not known how UDP-galactose is transported from the cytosol into the endoplasmic reticulum. We transfected ceramidegalactosyltransferase cDNA into CHOlec8 cells, which have a defective UGT and no endogenous ceramidegalactosyltransferase. Co-transfection with the human UGT1 greatly stimulated synthesis of lactosylceramide in the Golgi and of galactosylceramide in the endoplasmic reticulum. UDP-galactose was directly imported into the endoplasmic reticulum because transfection with UGT significantly enhanced synthesis of galactosylceramide in endoplasmic reticulum membranes. Subcellular fractionation and double label immunofluorescence microscopy showed that a sizeable fraction of ectopically expressed UGT and ceramidegalactosyltransferase resided in the endoplasmic reticulum of CHOlec8 cells. The same was observed when UGT was expressed in human intestinal cells which have an endogenous ceramidegalactosyltransferase. In contrast, in CHOlec8 singly transfected with UGT 1, the transporter localized exclusively to the Golgi complex. UGT and ceramidegalactosyltransferase were entirely detergent-soluble and form a complex since they could be co-immunoprecipitated. We conclude that the ceramidegalactosyltransferase ensures a supply of UDP-galactose in the endoplasmic reticulum lumen by retaining UGT in a molecular complex.
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