Oxidoreductases in Glycoprotein Glycosylation, Folding, and ERAD

Chaitanya Patel, Haddas Saad, Marina Shenkman, Gerardo Z. Lederkremer

Research output: Contribution to journalReview articlepeer-review

Abstract

N-linked glycosylation and sugar chain processing, as well as disulfide bond formation, are among the most common post-translational protein modifications taking place in the endoplasmic reticulum (ER). They are essential modifications that are required for membrane and secretory proteins to achieve their correct folding and native structure. Several oxidoreductases responsible for disulfide bond formation, isomerization, and reduction have been shown to form stable, functional complexes with enzymes and chaperones that are involved in the initial addition of an N-glycan and in folding and quality control of the glycoproteins. Some of these oxidoreductases are selenoproteins. Recent studies also implicate glycan machinery-oxidoreductase complexes in the recognition and processing of misfolded glycoproteins and their reduction and targeting to ER-associated degradation. This review focuses on the intriguing cooperation between the glycoprotein-specific cell machineries and ER oxidoreductases, and highlights open questions regarding the functions of many members of this large family.

Original languageEnglish
JournalCells
Volume9
Issue number9
DOIs
StatePublished - 22 Sep 2020

Keywords

  • ER quality control
  • ERAD
  • PDI
  • calnexin
  • mannosidase
  • oligosaccharyltransferase

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