Endoplasmic Reticulum Stress and Unfolded Protein Response Signaling in Plants

Hakim Manghwar, Jianming Li*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

30 Citations (Scopus)


Plants are sensitive to a variety of stresses that cause various diseases throughout their life cycle. However, they have the ability to cope with these stresses using different defense mechanisms. The endoplasmic reticulum (ER) is an important subcellular organelle, primarily recognized as a checkpoint for protein folding. It plays an essential role in ensuring the proper folding and maturation of newly secreted and transmembrane proteins. Different processes are activated when around one-third of newly synthesized proteins enter the ER in the eukaryote cells, such as glycosylation, folding, and/or the assembling of these proteins into protein complexes. However, protein folding in the ER is an error-prone process whereby various stresses easily interfere, leading to the accumulation of unfolded/misfolded proteins and causing ER stress. The unfolded protein response (UPR) is a process that involves sensing ER stress. Many strategies have been developed to reduce ER stress, such as UPR, ER-associated degradation (ERAD), and autophagy. Here, we discuss the ER, ER stress, UPR signaling and various strategies for reducing ER stress in plants. In addition, the UPR signaling in plant development and different stresses have been discussed.

Original languageEnglish
Article number828
Number of pages17
JournalInternational Journal of Molecular Sciences
Issue number2
Early online date13 Jan 2022
Publication statusPublished - Jan 2022

Scopus Subject Areas

  • Catalysis
  • Molecular Biology
  • Spectroscopy
  • Computer Science Applications
  • Physical and Theoretical Chemistry
  • Organic Chemistry
  • Inorganic Chemistry

User-Defined Keywords

  • plants
  • ER
  • ER stress
  • UPR
  • IRE1
  • bZIP17
  • bZIP28
  • bZIP60


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