Endoplasmic reticulum-mediated protein quality control in Arabidopsis

Yidan Liu, Jianming Li*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

83 Citations (Scopus)


A correct three-dimensional structure is crucial for the physiological functions of a protein, yet the folding of proteins to acquire native conformation is a fundamentally error-prone process. Eukaryotic organisms have evolved a highly conserved endoplasmic reticulum-mediated protein quality control (ERQC) mechanism to monitor folding processes of secretory and membrane proteins, allowing export of only correctly folded proteins to their physiological destinations, retaining incompletely/mis-folded ones in the ER for additional folding attempts, marking and removing terminally misfolded ones via a unique multiple-step degradation process known as ER-associated degradation (ERAD). Most of our current knowledge on ERQC and ERAD came from genetic and biochemical investigations in yeast and mammalian cells. Recent studies in the reference plant Arabidopsis thaliana uncovered homologous components and similar mechanisms in plants for monitoring protein folding and for retaining, repairing, and removing misfolded proteins. These studies also revealed critical roles of the plant ERQC/ERAD systems in regulating important biochemical/physiological processes, such as abiotic stress tolerance and plant defense. In this review, we discuss our current understanding about the molecular components and biochemical mechanisms of the plant ERQC/ERAD system in comparison to yeast and mammalian systems.

Original languageEnglish
Article number162
Number of pages11
JournalFrontiers in Plant Science
Issue numberAPR
Publication statusPublished - 30 Apr 2014

Scopus Subject Areas

  • Plant Science

User-Defined Keywords

  • Arabidopsis
  • Endoplasmic reticulum-mediated quality control
  • Endoplsamic reticulum-associated degradation
  • Misfolded glycoproteins
  • Receptor-like kinases


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