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Biochem Biophys Res Commun. 2013 May 10;434(3):473-8. doi: 10.1016/j.bbrc.2013.03.098. Epub 2013 Apr 10.

UDP-Gal/UDP-GlcNAc chimeric transporter complements mutation defect in mammalian cells deficient in UDP-Gal transporter.

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  • 1Laboratory of Biochemistry, Faculty of Biotechnology, University of Wrocław, 2 Tamka St, 50-137 Wrocław, Poland. Mariusz.Olczak@biotech.uni.wroc.pl

Abstract

The role of UDP-galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) in glycosylation of macromolecules may be coupled and either of the transporters may partially replace the function played by its partner. The aim of this study was to construct chimeric transporters composed of the N-terminal portion of human NGT and the C-terminal portion of human UGT1 or UGT2 (NGT-UGT1 or NGT-UGT2, respectively), as well as of the N-terminal portion of UGT and C-terminal portion of NGT (UGT-NGT), overexpress them stably in UGT-deficient CHO-Lec8 and MDCK-RCA(r) cells, and characterize their involvement in glycosylation. Two chimeric proteins, NGT-UGT1 and NGT-UGT2, did not overexpress properly. In contrast, UGT-NGT chimeric protein was successfully overexpressed and localized properly to the Golgi apparatus. UGT-NGT chimeric transporter delivered UDP-Gal to the Golgi vesicles of UGT-deficient cells, which resulted in the increased content of galactosylated structures to such an extent that the wild-type phenotypes were completely restored. Our data further support our hypothesis that UGT and NGT cooperate in the UDP-Gal delivery for glycosyltransferases located in the Golgi apparatus. In a wider context, the results gained in this study add to our understanding of glycosylation, one of the basic posttranslational modifications, which affects the majority of macromolecules.

Copyright © 2013 Elsevier Inc. All rights reserved.

PMID:
23583405
[PubMed - indexed for MEDLINE]
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