Related Experiment Video
Updated: May 21, 2026

Assaying Proteasomal Degradation in a Cell-free System in Plants
Published on: March 26, 2014
Endoplasmic reticulum-associated degradation of glycoproteins in plants
Silvia Hüttner1, Richard Strasser
1Department of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences Vienna, Austria.
Abstract:
In all eukaryotes the endoplasmic reticulum (ER) has a central role in protein folding and maturation of secretory and membrane proteins. Upon translocation into the ER polypeptides are immediately subjected to folding and modifications involving the formation of disulfide bridges, assembly of subunits to multi-protein complexes, and glycosylation. During these processes incompletely folded, terminally misfolded, and unassembled proteins can accumulate which endanger the cellular homeostasis and subsequently the survival of cells and tissues. Consequently, organisms have developed a quality control system to cope with this problem and remove the unwanted protein load from the ER by a process collectively referred to as ER-associated degradation (ERAD) pathway. Recent studies in Arabidopsis have identified plant ERAD components involved in the degradation of aberrant proteins and evidence was provided for a specific role in abiotic stress tolerance. In this short review we discuss our current knowledge about this important cellular pathway.
Related Concept Videos
Export of Misfolded Proteins out of the ER
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Protein Folding Quality Check in the RER
The Unfolded Protein Response
Cell Signaling in Plants

