Endoplasmic reticulum retention of the large splice variant of the UDP-galactose transporter is caused by a dilysine motif.

@article{Kabuss2005EndoplasmicRR,
  title={Endoplasmic reticulum retention of the large splice variant of the UDP-galactose transporter is caused by a dilysine motif.},
  author={Roland Kabuss and Angel Ashikov and Stefan Oelmann and Rita Gerardy-Schahn and Hans Bakker},
  journal={Glycobiology},
  year={2005},
  volume={15 10},
  pages={
          905-11
        }
}
Nucleotide-sugar transporters supply mainly the Golgi glycosyltransferases with substrates. Some glycosyltransferases in the endoplasmic reticulum (ER), however, also use activated sugars. Recent studies have demonstrated that UDP-galactose (UDP-Gal) is the substrate for the ER resident ceramide-galactosyltransferase (cer-GalT) and cells expressing cer-GalT are able to retain the UDP-Gal transporter (UGT) by physical contacts formed between the two proteins. Here, we describe a second active… CONTINUE READING

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