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Annual Review of Plant Biology

Volume 69, 2018

Protein Quality Control in the Endoplasmic Reticulum of Plants

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.

Keyword(s): endoplasmic reticulum–associated degradation, ERAD, ERQC, glycoprotein, glycosylation, protein folding
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2018-04-29
2024-04-18
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Protein Quality Control in the Endoplasmic Reticulum of Plants
Annual Review of Plant Biology 69, 147 (2018); https://doi.org/10.1146/annurev-arplant-042817-040331
/content/journals/10.1146/annurev-arplant-042817-040331
/content/journals/10.1146/annurev-arplant-042817-040331
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