Evidence map›Paper›PMID 23509268›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

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

Kei-ichiro Mishiba, Yukihiro Nagashima, Eiji Suzuki, Noriko Hayashi, Yoshiyuki Ogata, Yukihisa Shimada, Nozomu Koizumi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
103citing papers in PubMed, 2 pooled it
7.8field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

103 citing papers in PubMed, 2 syntheses or guidelines pooled it, 176 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Review
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  5. Article
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  12. Review
  13. In-Depth Characterization ofPlants (Basel, Switzerland) · 2024
    Article
  14. Article
  15. Article
  16. Unfolded Protein Response in Arabidopsis.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  17. Article
  18. Mechanisms of Endoplasmic Reticulum Protein Homeostasis in Plants.International journal of molecular sciences · 2023
    Review
  19. Review
  20. Article

43 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Kei-ichiro MishibaDivision of Applied Life Sciences, Graduate School of Life and Environmental Sciences, Osaka Prefecture University, Nakaku, Sakai, Osaka 599-8531, Japan.
Yukihiro Nagashima
Eiji Suzuki
Noriko Hayashi
Yoshiyuki Ogata
Yukihisa Shimada
Nozomu Koizumi
Osaka Prefecture University · JPYokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolded protein response (UPR) is a cellular response highly conserved in eukaryotes to obviate accumulation of misfolded proteins in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 (IRE1) catalyzes the cytoplasmic splicing of mRNA encoding bZIP transcription factors to activate the UPR signaling pathway. Arabidopsis IRE1 was recently shown to be involved in the cytoplasmic splicing of bZIP60 mRNA. In the present study, we demonstrated that an Arabidopsis mutant with defects in two IRE1 paralogs showed enhanced cell death upon ER stress compared with a mutant with defects in bZIP60 and wild type, suggesting an alternative function of IRE1 in the UPR. Analysis of our previous microarray data and subsequent quantitative PCR indicated degradation of mRNAs encoding secretory pathway proteins by tunicamycin, DTT, and heat in an IRE1-dependent manner. The degradation of mRNAs localized to the ER during the UPR was considered analogous to a molecular mechanism referred to as the regulated IRE1-dependent decay of mRNAs reported in metazoans. Another microarray analysis conducted in the condition repressing transcription with actinomycin D and a subsequent Gene Set Enrichment Analysis revealed the regulated IRE1-dependent decay of mRNAs-mediated degradation of a significant portion of mRNAs encoding the secretory pathway proteins. In the mutant with defects in IRE1, genes involved in the cytosolic protein response such as heat shock factor A2 were up-regulated by tunicamycin, indicating the connection between the UPR and the cytosolic protein response.

Indexed as

ArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsComputational BiologyDNA FragmentationEndoplasmic Reticulum StressEvans BlueGene Expression Regulation, PlantMicroarray AnalysisMutationProtein KinasesRNA StabilityTunicamycinUnfolded Protein ResponseArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsEvans BlueIre1-1 protein, ArabidopsisProtein KinasesTunicamycin

Identifiers

PMID23509268
PMCPMC3619347
OpenAlexW2132082002

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.