UDP-N-acetylglucosamine transporter and UDP-galactose transporter form heterologous complexes in the Golgi membrane

FEBS Lett. 2012 Nov 30;586(23):4082-7. doi: 10.1016/j.febslet.2012.10.016. Epub 2012 Oct 23.

Abstract

UDP-galactose transporter (UGT; SLC35A2) and UDP-N-acetylglucosamine transporter (NGT; SLC35A3) are evolutionarily related. We hypothesize that their role in glycosylation may be coupled through heterologous complex formation. Coimmunoprecipitation analysis and FLIM-FRET measurements performed on living cells showed that NGT and UGT form complexes when overexpressed in MDCK-RCA(r) cells. We also postulate that the interaction of NGT and UGT may explain the dual localization of UGT2. For the first time we demonstrated in vivo homodimerization of the NGT nucleotide sugar transporter. In conclusion, we suggest that NGT and UGT function in glycosylation is combined via their mutual interaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Dogs
  • Golgi Apparatus / metabolism*
  • Immunoprecipitation
  • Membrane Transport Proteins / genetics
  • Membrane Transport Proteins / metabolism*
  • Monosaccharide Transport Proteins / genetics
  • Monosaccharide Transport Proteins / metabolism*
  • Protein Binding

Substances

  • Membrane Transport Proteins
  • Monosaccharide Transport Proteins
  • UDP-N-acetylglucosamine transporter
  • UDP-galactose translocator