| First Author | Trombetta ES | Year | 1999 |
| Journal | EMBO J | Volume | 18 |
| Issue | 12 | Pages | 3282-92 |
| PubMed ID | 10369669 | Mgi Jnum | J:65756 |
| Mgi Id | MGI:1927266 | Doi | 10.1093/emboj/18.12.3282 |
| Citation | Trombetta ES, et al. (1999) Glycoprotein reglucosylation and nucleotide sugar utilization in the secretory pathway: identification of a nucleoside diphosphatase in the endoplasmic reticulum. EMBO J 18(12):3282-92 |
| abstractText | 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 hydrolyzes UDP, GDP and IDP but not any other nucleoside di-, mono- or triphosphates, nor thiamine pyrophosphate. By eliminating UDP, which is an inhibitory product of the UDP-Glc:glycoprotein glucosyltransferase, it is likely to promote reglucosylation reactions involved in glycoprotein folding and quality control in the ER. |
