Evidence map›Paper›PMID 24923602›Full record

ArticleMolecular plant2014

Salicylic acid signaling controls the maturation and localization of the arabidopsis defense protein ACCELERATED CELL DEATH6.

Zhongqin Zhang, Jay Shrestha, Chika Tateda, Jean T Greenberg

Open access · bronzeAbstract read
In one paragraph

Article in Molecular plant, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 17% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 49 citations in OpenAlex.

  1. Pooled it
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  5. Genetic Analyses of Seed Longevity inPlants (Basel, Switzerland) · 2023
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  14. Transcription of lncRNARNA biology · 2020
    Article
  15. Identification and characterization of maizePlant signaling & behavior · 2019
    Article
  16. Article
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  18. Review
  19. Article
  20. Review
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

4 authors at 1 institution in 1 country.

Zhongqin ZhangDepartment of Molecular Genetics and Cell Biology, University of Chicago, 929 East 57 Street, GCIS W524, Chicago, IL 60637, USA.
Jay ShresthaDepartment of Molecular Genetics and Cell Biology, University of Chicago, 929 East 57 Street, GCIS W524, Chicago, IL 60637, USA.
Chika TatedaDepartment of Molecular Genetics and Cell Biology, University of Chicago, 929 East 57 Street, GCIS W524, Chicago, IL 60637, USA.
Jean T GreenbergDepartment of Molecular Genetics and Cell Biology, University of Chicago, 929 East 57 Street, GCIS W524, Chicago, IL 60637, USA. Electronic address: jgreenbe@uchicago.edu.
University of Chicago · US

Funding

Re-Engineering Translational Research at the University of ChicagoUL1TR000430 · NCATS · UNIVERSITY OF CHICAGO · PI SOLWAY, JULIAN · 2012 to 2016
$20.2M
Molecular Basis of Pathogen-Induced Cell Death in PlantsR01GM054292 · NIGMS · UNIVERSITY OF CHICAGO · PI GREENBERG, JEAN T. · 2001 to 2009
$2.6M
NCATS NIH HHS UL1 TR000430NIGMS NIH HHS R01 GM054292NIGMS NIH HHS R01 GM54292
6 · The paper itself

Abstract

ACCELERATED CELL DEATH6 (ACD6) is a multipass membrane protein with an ankyrin domain that acts in a positive feedback loop with the defense signal salicylic acid (SA). This study implemented biochemical approaches to infer changes in ACD6 complexes and localization. In addition to forming endoplasmic reticulum (ER)- and plasma membrane (PM)-localized complexes, ACD6 forms soluble complexes, where it is bound to cytosolic HSP70, ubiquitinated, and degraded via the proteasome. Thus, ACD6 constitutively undergoes ER-associated degradation. During SA signaling, the soluble ACD6 pool decreases, whereas the PM pool increases. Similarly, ACD6-1, an activated version of ACD6 that induces SA, is present at low levels in the soluble fraction and high levels in the PM. However, ACD6 variants with amino acid substitutions in the ankyrin domain form aberrant, inactive complexes, are induced by a SA agonist, but show no PM localization. SA signaling also increases the PM pools of FLAGELLIN SENSING2 (FLS2) and BRI1-ASSOCIATED RECEPTOR KINASE 1 (BAK1). FLS2 forms complexes ACD6; both FLS2 and BAK1 require ACD6 for maximal accumulation at the PM in response to SA signaling. A plausible scenario is that SA increases the efficiency of productive folding and/or complex formation in the ER, such that ACD6, together with FLS2 and BAK1, reaches the cell surface to more effectively promote immune responses.

Indexed as

Signal TransductionAmino Acid SequenceAnkyrinsArabidopsisArabidopsis ProteinsCell MembraneEndoplasmic ReticulumEnzyme ActivationHSP70 Heat-Shock ProteinsMolecular Sequence DataMutationProteasome Endopeptidase ComplexProtein Structure, TertiaryProtein TransportProteolysisSalicylic AcidACD6 protein, ArabidopsisAnkyrinsArabidopsis ProteinsHSP70 Heat-Shock ProteinsProteasome Endopeptidase ComplexSalicylic AcidACD6protein quality controlprotein traffickingsalicylic acid

Identifiers

PMID24923602
PMCPMC4168298
OpenAlexW1558452662

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.