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

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


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • CHO Cells
  • Cricetulus
  • Dogs
  • Galactose / metabolism*
  • Glycosylation
  • Humans
  • Madin Darby Canine Kidney Cells
  • Monosaccharide Transport Proteins / metabolism*
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism*


  • Monosaccharide Transport Proteins
  • Polysaccharides
  • UDP-galactose translocator
  • Galactose