Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum

@article{Trombetta1999GlycoproteinRA,
  title={Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum},
  author={E. Sergio Trombetta and Ari Helenius},
  journal={The EMBO Journal},
  year={1999},
  volume={18}
}
UDP is generated in the lumen of the endoplasmic reticulum (ER) as a product of the UDP‐glucose‐dependent glycoprotein reglucosylation in the calnexin/calreticulin cycle. We describe here the identification, purification and characterization of an ER enzyme that hydrolyzes UDP to UMP. This nucleoside diphosphatase is a ubiquitously expressed, soluble 45 kDa glycoprotein devoid of transmembrane domains and KDEL‐related ER localization sequences. It requires divalent cations for activity and… Expand
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