Protein Folding in the Endoplasmic Reticulum
- 1Cellular Protein Chemistry, Faculty of Science, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands
- 2Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003
- Correspondence: i.braakman{at}uu.nl; dhebert{at}biochem.umass.edu
Abstract
In this article, we will cover the folding of proteins in the lumen of the endoplasmic reticulum (ER), including the role of three types of covalent modifications: signal peptide removal, N-linked glycosylation, and disulfide bond formation, as well as the function and importance of resident ER folding factors. These folding factors consist of classical chaperones and their cochaperones, the carbohydrate-binding chaperones, and the folding catalysts of the PDI and proline cis–trans isomerase families. We will conclude with the perspective of the folding protein: a comparison of characteristics and folding and exit rates for proteins that travel through the ER as clients of the ER machinery.
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