Evidence map›Paper›PMID 29760094›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Salicylic acid-independent role of NPR1 is required for protection from proteotoxic stress in the plant endoplasmic reticulum.

Ya-Shiuan Lai, Luciana Renna, John Yarema, Cristina Ruberti, Sheng Yang He, Federica Brandizzi

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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
3.8field-weighted citation impact, top 6% 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, 85 citations in OpenAlex.

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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

6 authors at 2 institutions in 1 country.

Ya-Shiuan LaiMichigan State University-US Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824.
Luciana RennaMichigan State University-US Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824.
John YaremaMichigan State University-US Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824.
Cristina RubertiMichigan State University-US Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824.ORCID 0000-0002-9013-1412
Sheng Yang HeMichigan State University-US Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824.
Federica BrandizziMichigan State University-US Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824; fb@msu.edu.ORCID 0000-0002-5047-1068
Michigan State University · USHoward Hughes Medical Institute · US

Funding

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

Abstract

The unfolded protein response (UPR) is an ancient signaling pathway designed to protect cells from the accumulation of unfolded and misfolded proteins in the endoplasmic reticulum (ER). Because misregulation of the UPR is potentially lethal, a stringent surveillance signaling system must be in place to modulate the UPR. The major signaling arms of the plant UPR have been discovered and rely on the transcriptional activity of the transcription factors bZIP60 and bZIP28 and on the kinase and ribonuclease activity of IRE1, which splices mRNA to activate bZIP60. Both bZIP28 and bZIP60 modulate UPR gene expression to overcome ER stress. In this study, we demonstrate at a genetic level that the transcriptional role of bZIP28 and bZIP60 in ER-stress responses is antagonized by nonexpressor of PR1 genes 1 (NPR1), a critical redox-regulated master regulator of salicylic acid (SA)-dependent responses to pathogens, independently of its role in SA defense. We also establish that the function of NPR1 in the UPR is concomitant with ER stress-induced reduction of the cytosol and translocation of NPR1 to the nucleus where it interacts with bZIP28 and bZIP60. Our results support a cellular role for NPR1 as well as a model for plant UPR regulation whereby SA-independent ER stress-induced redox activation of NPR1 suppresses the transcriptional role of bZIP28 and bZIP60 in the UPR.

Indexed as

ArabidopsisArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsEndoplasmic ReticulumEndoplasmic Reticulum StressSalicylic AcidUnfolded Protein ResponseArabidopsis ProteinsBasic-Leucine Zipper Transcription FactorsbZIP28 protein, ArabidopsisbZIP60 protein, ArabidopsisNPR1 protein, ArabidopsisSalicylic Acidendoplasmic reticulumNPR1salicylic acidunfolded protein response

Identifiers

PMID29760094
PMCPMC5984531
OpenAlexW2804090259

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.