Format

Send to

Choose Destination
Traffic. 2016 Jun;17(6):615-38. doi: 10.1111/tra.12392. Epub 2016 Apr 22.

Co- and Post-Translational Protein Folding in the ER.

Author information

1
Department of Biology, University of Copenhagen, Copenhagen, Denmark.
2
Cellular Protein Chemistry, Faculty of Science, Utrecht University, Utrecht, The Netherlands.

Abstract

The biophysical rules that govern folding of small, single-domain proteins in dilute solutions are now quite well understood. The mechanisms underlying co-translational folding of multidomain and membrane-spanning proteins in complex cellular environments are often less clear. The endoplasmic reticulum (ER) produces a plethora of membrane and secretory proteins, which must fold and assemble correctly before ER exit - if these processes fail, misfolded species accumulate in the ER or are degraded. The ER differs from other cellular organelles in terms of the physicochemical environment and the variety of ER-specific protein modifications. Here, we review chaperone-assisted co- and post-translational folding and assembly in the ER and underline the influence of protein modifications on these processes. We emphasize how method development has helped advance the field by allowing researchers to monitor the progression of folding as it occurs inside living cells, while at the same time probing the intricate relationship between protein modifications during folding.

KEYWORDS:

N-glycosylation; chaperones; disulfide-bond formation; endoplasmic reticulum; folding enzymes; protein folding

PMID:
26947578
DOI:
10.1111/tra.12392
[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center