Evidence map›Paper›PMID 29124827›Full record

ArticleThe Plant journal : for cell and molecular biology2018

Recovery from temporary endoplasmic reticulum stress in plants relies on the tissue-specific and largely independent roles of bZIP28 and bZIP60, as well as an antagonizing function of BAX-Inhibitor 1 upon the pro-adaptive signaling mediated by bZIP28.

Cristina Ruberti, YaShiuan Lai, Federica Brandizzi

Open access · bronzeAbstract read
In one paragraph

Article in The Plant journal : for cell and molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed, 1 pooled it
3.4field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 1 synthesis or guideline pooled it, 65 citations in OpenAlex.

  1. Pooled it
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  14. CRISPR/Cas9-MediatedInternational journal of molecular sciences · 2023
    Article
  15. Systematic evolution ofFrontiers in plant science · 2023
    Article
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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

3 authors at 1 institution in 1 country.

Cristina RubertiPlant Research Laboratory, Department of Energy, Michigan State University, 612 Wilson Road, East Lansing, MI, 48824, USA.ORCID http://orcid.org/0000-0002-9013-1412
YaShiuan LaiPlant Research Laboratory, Department of Energy, Michigan State University, 612 Wilson Road, East Lansing, MI, 48824, USA.
Federica BrandizziPlant Research Laboratory, Department of Energy, Michigan State University, 612 Wilson Road, East Lansing, MI, 48824, USA.ORCID http://orcid.org/0000-0003-0580-8888
Michigan State University · US

Funding

Unfolded protein response in the model species Arabidopsis thalianaR01GM101038 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BRANDIZZI, FEDERICA · 2012 to 2019
$2.5M
NIGMS NIH HHS R01 GM101038
6 · The paper itself

Abstract

The unfolded protein response (UPR) is an ancient signaling pathway that commits to life-or-death outcomes in response to proteotoxic stress in the endoplasmic reticulum (ER). In plants, the membrane-tethered transcription factor bZIP28 and the ribonuclease-kinase IRE1 along with its splicing target, bZIP60, govern the two cytoprotective UPR signaling pathways known to date. The conserved ER membrane-associated BAX inhibitor 1 (BI1) modulates ER stress-induced programmed cell death through yet-unknown mechanisms. Despite the significance of the UPR for cell homeostasis, in plants the regulatory circuitry underlying ER stress resolution is still largely unmapped. To gain insights into the coordination of plant UPR strategies, we analyzed the functional relationship of the UPR modulators through the analysis of single and higher order mutants of IRE1, bZIP60, bZIP28 and BI1 in experimental conditions causing either temporary or chronic ER stress. We established a functional duality of bZIP28 and bZIP60, as they exert partially independent tissue-specific roles in recovery from ER stress, but redundantly actuate survival strategies in chronic ER stress. We also discovered that BI1 attenuates the pro-survival function of bZIP28 in ER stress resolution and, differently to animal cells, it does not temper the ribonuclease activity of inositol-requiring enzyme 1 (IRE1) under temporary ER stress. Together these findings reveal a functional independence of bZIP28 and bZIP60 in plant UPR, and identify an antagonizing role of BI1 in the pro-adaptive signaling mediated by bZIP28, bringing to light the distinctive complexity of the unfolded protein response (UPR) in plants.

Indexed as

Endoplasmic Reticulum StressSignal TransductionUnfolded Protein ResponseArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsEndoplasmic ReticulumGene Expression Regulation, PlantRNA SplicingArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsbZIP28 protein, ArabidopsisbZIP60 protein, ArabidopsisArabidopsisBI1bZIP28bZIP60IRE1unfolded protein response

Identifiers

PMID29124827
PMCPMC5732024
OpenAlexW2767254956

What OpenQuestion holds

Textmetadata
LicenceTDM
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.