Glycan dependent refolding activity of ER glucosyltransferase (UGGT)

• Published in: Biochimica et biophysica acta. General subjects Vol. 1864; no. 12; p. 129709
• Main Authors: Wang, Ning, Seko, Akira, Takeda, Yoichi, Ito, Yukishige
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.12.2020
• Subjects: endoplasmic reticulum; Endoplasmic reticulum quality control; Glucosyltransferases - metabolism; Glycoprotein folding; Glycoprotein glucosyltransferase; glycoproteins; Glycosylation; Humans; Mannose - metabolism; mutants; Oligomannose-type glycan; Polysaccharides - metabolism; Protein Denaturation; Protein Folding; Protein Refolding; quality control; Ribonuclease; ribonucleases; Ribonucleases - metabolism; RNA; Substrate Specificity; UDP-glucose; Endoplasmic reticulum quality control; Glycoprotein folding; Glycoprotein glucosyltransferase; Ribonuclease; Oligomannose-type glycan; UDP-glucose

In the endoplasmic reticulum (ER), folding of glycoproteins is assisted by a combined action of enzymes and chaperones that leads them to biologically functional structures. In this system, UDP-glucose:glycoprotein glucosyltransferase 1 (UGGT1) plays an essential role as the “folding sensor” by virt...