Defects in IRE1 enhance cell death and fail to degrade mRNAs encoding secretory pathway proteins in the
            <i>Arabidopsis</i>
            unfolded protein response

Mishiba, Kei‐ichiro; Nagashima, Yukihiro; Suzuki, Eiji; Hayashi, Noriko; Ogata, Yasuhiro; Shimada, Yukihisa; Koizumi, Nozomu

doi:10.1073/pnas.1219047110

Cited by 169 publications

(183 citation statements)

References 53 publications

(60 reference statements)

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“…Mishiba et al (12) recently reported that RIDD is required for the ER stress tolerance in Arabidopsis. They showed that the mRNAs for a set of secreted proteins were degraded in response to ER stress.…”

Section: Discussionmentioning

confidence: 99%

“…Mishiba et al (12) recently showed that IRE1 is also involved in RIDD, a process by which mRNAs encoding secreted proteins on membrane-bound ribosomes are degraded in response to stress. In addition, they identified several RIDD target mRNAs in Arabidopsis.…”

Section: Significancementioning

confidence: 99%

“…Up to this time, the analysis of single mutants in the pathway had not revealed functions for the UPR in plant growth and stress tolerance, although an ire1a ire1b double mutant was found to show a modest short root phenotype and increased sensitivity to ER stress agents (12). The lack of distinctive phenotypes led us to question whether the UPR really plays an important role in plant growth or stress tolerance.…”

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confidence: 99%

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Protein kinase and ribonuclease domains of IRE1 confer stress tolerance, vegetative growth, and reproductive development in Arabidopsis

Deng

Srivastava

Howell

2013

Proc. Natl. Acad. Sci. U.S.A.

118

189

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The unfolded protein response (UPR) endows plants with the capacity to perceive, respond, and protect themselves from adverse environmental conditions. The UPR signaling pathway in Arabidopsis has two "arms," one arm involving the bifunctional protein kinase (PK)/ribonuclease, IRE1, a RNA splicing enzyme, and another involving membrane-associated transcription factors, such as basic leucine zipper transcription factor 28 (bZIP28). Because of functional redundancies, single gene mutations in the plant UPR signaling pathway generally have not resulted in prominent phenotypes. In this study we generated multiple mutations in the UPR signaling pathway, such as an ire1a ire1b double mutant, which showed defects in stress tolerance and vegetative growth and development. Complementation of ire1a ire1b with constructs containing site-specific mutations in the PK or RNase domains of IRE1b demonstrated that a functional RNase domain is required for endoplasmic reticulum stress tolerance, and that both the PK and RNase domains are required for normal vegetative growth under unstressed conditions. Root growth under stress conditions was dependent on the splicing target of IRE1b, bZIP60 mRNA, and on regulated IRE1-dependent decay of target genes. However, root and shoot growth in the absence of stress was independent of bZIP60. Blocking both arms of the UPR signaling pathway in a triple ire1a ire1b bzip28 mutant was lethal, impacting pollen viability under unstressed conditions. Complementation with IRE1b constructs showed that both the PK and RNase domains are required for normal gametophyte development, but bZIP60 is not. Hence, the UPR plays a critical role in stress tolerance, and in normal vegetative growth and reproductive development in plants.T he plant unfolded protein response (UPR) is important in protecting plants from environmental stress. Adverse environmental conditions can interfere with sensitive biosynthetic processes in plants such as protein folding. The UPR has been subject of many recent reviews (for example, see ref. 1) and results from the accumulation of misfolded proteins in the endoplasmic reticulum (ER). The UPR signaling pathway in plants consists of two "arms," one involving membrane associated transcription factors such as basic leucine zipper transcription factor 17 and 28 (bZIP17 and bZIP28) and another arm involving Inositol requiring enzyme1 (IRE1) (2). IRE1 is a dual PK/ribonuclease that is conserved from yeast to man. In response to stress, IRE1 is activated and splices a specific target mRNA in the cytoplasm that encodes a stress-response transcription factor.IRE1 is a single-pass transmembrane protein in the ER membrane with its N terminus facing the ER lumen, serving as a sensor domain. The C terminus of the protein faces the cytosol and contains the PK and ribonuclease domains. Upon activation, IRE1 dimerizes or oligomerizes and undergoes transphosphorylation and activation of its ribonuclease domain (3, 4). Splicing involves cleavage in each of two loops of the substrate RNA, removal...

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Section: Discussionmentioning

confidence: 99%

Section: Significancementioning

confidence: 99%

mentioning

confidence: 99%

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Protein kinase and ribonuclease domains of IRE1 confer stress tolerance, vegetative growth, and reproductive development in Arabidopsis

Deng

Srivastava

Howell

2013

Proc. Natl. Acad. Sci. U.S.A.

118

189

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“…3,12,13 In view of these findings, OsIRE1 may play other important roles in addition to OsbZIP50 mRNA splicing and its function may be species specific.…”

Section: Discussionmentioning

confidence: 99%

Effect of overexpression of kinase- or RNase-deficient OsIRE1 on the endoplasmic reticulum stress response in transgenic rice plants

Wakasa¹,

Hayashi²,

Takaiwa

2013

Plant Signaling & Behavior

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“…In addition, IRE1A and IRE1B function in RIDD (Mishiba et al 2013) as in other organisms. A broad range of mRNAs encoding secretory and membrane proteins are destabilized through RIDD in Arabidopsis.…”

mentioning

confidence: 99%

Inositol-requiring enzyme 1 affects meristematic division in roots under moderate salt stress in Arabidopsis

Iwata

Yagi

Saito

et al. 2017

Plant Biotechnology

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The unfolded protein response (UPR) mitigates stress caused by accumulation of unfolded proteins in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 (IRE1) is the most conserved sensor of the UPR with ribonuclease activity that mediates cytoplasmic splicing and decay of mRNA encoding secretory and membrane proteins. In the present study, we demonstrate that the Arabidopsis mutant defective in two IRE1 genes exhibit retarded growth of primary roots under moderate salt stress, although such grow retardation is not observed in wild type plants. Microscopic observation showed decrease in the number of meristematic cells in the mutant under salt stress. This finding suggests that IRE1 plays a role in the maintenance of root meristems under salt stress. Possible connections between the function of IRE1 and the salt sensitivity are discussed.

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Defects in IRE1 enhance cell death and fail to degrade mRNAs encoding secretory pathway proteins in the Arabidopsis unfolded protein response

Cited by 169 publications

References 53 publications

Protein kinase and ribonuclease domains of IRE1 confer stress tolerance, vegetative growth, and reproductive development in Arabidopsis

Protein kinase and ribonuclease domains of IRE1 confer stress tolerance, vegetative growth, and reproductive development in Arabidopsis

Effect of overexpression of kinase- or RNase-deficient OsIRE1 on the endoplasmic reticulum stress response in transgenic rice plants

Inositol-requiring enzyme 1 affects meristematic division in roots under moderate salt stress in Arabidopsis

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