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Biochem Biophys Res Commun. 2014 Nov 28;454(4):486-92. doi: 10.1016/j.bbrc.2014.10.098. Epub 2014 Oct 28.

Short N-terminal region of UDP-galactose transporter (SLC35A2) is crucial for galactosylation of N-glycans.

Author information

1
Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, 14A F. Joliot-Curie St., 50-383 Wroclaw, Poland.
2
Laboratory of Biotechnology, Faculty of Biotechnology, University of Wroclaw, 14A F. Joliot-Curie St., 50-383 Wroclaw, Poland.
3
Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, 14A F. Joliot-Curie St., 50-383 Wroclaw, Poland. Electronic address: Mariusz.Olczak@biotech.uni.wroc.pl.

Abstract

UDP-galactose transporter (UGT) and UDP-N-acetylglucosamine transporter (NGT) form heterologous complexes in the Golgi apparatus (GA) membrane. We aimed to identify UGT region responsible for galactosylation of N-glycans. Chimeric proteins composed of human UGT and either NGT or CMP-sialic acid transporter (CST) localized to the GA, and all but UGT/CST chimera corrected galactosylation defect in UGT-deficient cell lines, although at different efficiency. Importantly, short N-terminal region composed of 35 N-terminal amino-acid residues of UGT was crucial for galactosylation of N-glycans. The remaining molecule must be derived from NGT not CST, confirming that the role played by UGT and NGT is coupled.

KEYWORDS:

Chimeric protein; Glycosylation; Golgi apparatus; UDP-N-acetylglucosamine transporter; UDP-galactose transporter

PMID:
25451267
DOI:
10.1016/j.bbrc.2014.10.098
[Indexed for MEDLINE]

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