J Integr Plant Biol. ›› 2017, Vol. 59 ›› Issue (7): 506-521.DOI: 10.1111/jipb.12544

• Plant-environmental Interactions • Previous Articles    

Unfolded protein response activation compensates endoplasmic reticulum-associated degradation deficiency in Arabidopsis

Qingliang Li1†, Hai Wei1,2†, Lijing Liu1, Xiaoyuan Yang1, Xiansheng Zhang2 and Qi Xie1*   

  1. 1State Key Laboratory of Plant Genomics, National Center for Plant Gene Research, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China
    2State Key Laboratory of Crop Biology, Shandong Key Laboratory of Crop Biology, College of Life Sciences, Shandong Agricultural University, Taian 271018, China
  • Received:2017-02-17 Accepted:2017-04-10 Published:2017-04-18
  • About author:These authors contributed equally to this work
    *correspondence: E-mail: Qi Xie (qxie@genetics.ac.cn)


Abiotic stresses often disrupt protein folding and induce endoplasmic reticulum (ER) stress. There is a sophisticated ER quality control (ERQC) system to mitigate the effects of malfunctioning proteins and maintain ER homeostasis. The accumulation of misfolded proteins in the ER activates the unfolded protein response (UPR) to enhance ER protein folding and the degradation of misfolded proteins mediate by ER-associated degradation (ERAD). That ERQC reduces abiotic stress damage has been well studied in mammals and yeast. However, in plants, both ERAD and UPR have been studied separately and found to be critical for plant abiotic stress tolerance. In this study, we discovered that UPR-associated transcription factors AtbZIP17, AtbZIP28 and AtbZIP60 responded to tunicamycin (TM) and NaCl induced ER stress and subsequently enhanced Arabidopsis thaliana abiotic stress tolerance. They regulated the expression level of ER chaperones and the HRD1-complex components. Moreover, overexpression of AtbZIP17, AtbZIP28 and AtbZIP60 could restore stress tolerance via ERAD in the HRD1-complex mutant hrd3a-2, which suggested that UPR and ERAD have an interactive mechanism in Arabidopsis.

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