Abstract
Maintenance of proteome integrity is essential for cell function and survival in changing cellular and environmental conditions. The endoplasmic reticulum (ER) is the major site for the synthesis of secretory and membrane proteins. However, the accumulation of unfolded or misfolded proteins can perturb ER protein homeostasis, leading to ER stress and compromising cellular function. Eukaryotic organisms have evolved sophisticated and conserved protein quality control systems to ensure protein folding fidelity via the unfolded protein response (UPR) and to eliminate potentially harmful proteins via ER-associated degradation (ERAD) and ER-phagy. In this review, we summarize recent advances in our understanding of the mechanisms of ER protein homeostasis in plants and discuss the crosstalk between different quality control systems. Finally, we will address unanswered questions in this field.
Original language | English |
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Article number | 17599 |
Number of pages | 15 |
Journal | International Journal of Molecular Sciences |
Volume | 24 |
Issue number | 24 |
DOIs | |
Publication status | Published - 2 Dec 2023 |
Scopus Subject Areas
- Catalysis
- Molecular Biology
- Spectroscopy
- Computer Science Applications
- Physical and Theoretical Chemistry
- Organic Chemistry
- Inorganic Chemistry
User-Defined Keywords
- ER homeostasis
- unfolded protein response (UPR)
- ER-associated degradation (ERAD)
- ER-phagy
- Arabidopsis thaliana