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Annu Rev Plant Biol. 2018 Apr 29;69:147-172. doi: 10.1146/annurev-arplant-042817-040331. Epub 2018 Mar 23.

Protein Quality Control in the Endoplasmic Reticulum of Plants.

Author information

1
Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, 1190 Vienna, Austria; email: richard.strasser@boku.ac.at.

Abstract

The endoplasmic reticulum (ER) is the site of maturation for roughly one-third of all cellular proteins. ER-resident molecular chaperones and folding catalysts promote folding and assembly in a diverse set of newly synthesized proteins. Because these processes are error-prone, all eukaryotic cells have a quality-control system in place that constantly monitors the proteins and decides their fate. Proteins with potentially harmful nonnative conformations are subjected to assisted folding or degraded. Persistent folding-defective proteins are distinguished from folding intermediates and targeted for degradation by a specific process involving clearance from the ER. Although the basic principles of these processes appear conserved from yeast to animals and plants, there are distinct differences in the ER-associated degradation of misfolded glycoproteins. The general importance of ER quality-control events is underscored by their involvement in the biogenesis of diverse cell surface receptors and their crucial maintenance of protein homeostasis under diverse stress conditions.

KEYWORDS:

ERAD; ERQC; endoplasmic reticulum–associated degradation; glycoprotein; glycosylation; protein folding

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