Glycoprotein folding in the endoplasmic reticulum: A tale of three chaperones?

Stephen High, Fabienne J L Lecomte, Sarah J. Russell, Benjamin M. Abell, Jason D. Oliver

Research output: Contribution to journalArticlepeer-review

Abstract

The endoplasmic reticulum (ER) is a major site of protein synthesis and its inside, or lumen, is a major site of protein folding. The lumen of the ER contains many folding factors and molecular chaperones, which facilitate protein folding by increasing both the rate and the efficiency of this process. Amongst the many ER folding factors, there are three components that specifically modulate the folding glycoproteins bearing N-linked carbohydrate side chains. These components are calnexin, calreticulin and ERp57, and this review focuses on the molecular basis for their capacity to influence glycoprotein folding. Copyright (C) 2000 Federation of European Biochemical Societies.
Original languageEnglish
Pages (from-to)38-41
Number of pages3
JournalFEBS Letters
Volume476
Issue number1-2
DOIs
Publication statusPublished - 30 Jun 2000

Keywords

  • Calnexin
  • Endoplasmic reticulum
  • ERp57
  • Glycoprotein
  • Molecular chaperone
  • Protein folding

Research Beacons, Institutes and Platforms

  • Manchester Institute of Biotechnology

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