Evidence map›Paper›PMID 22021419›Full record

ArticlePlant physiology2011

A plant small polypeptide is a novel component of DNA-binding protein phosphatase 1-mediated resistance to plum pox virus in Arabidopsis.

María José Castelló, Jose Luis Carrasco, Marisa Navarrete-Gómez, Jacques Daniel, David Granot, Pablo Vera

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 20% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Abiotic Stress in Crop Production.International journal of molecular sciences · 2023
    Pooled it
  2. Bacterial Volatiles (mVOC) Emitted by the PhytopathogenAntioxidants (Basel, Switzerland) · 2023
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
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 3 institutions in 2 countries.

María José CastellóInstituto de Biología Molecular y Celular de Plantas, Universidad Politécnica de Valencia-Consejo Superior de Investigaciones Científicas, 46022 Valencia, Spain.
Jose Luis Carrasco
Marisa Navarrete-Gómez
Jacques Daniel
David Granot
Pablo Vera
Centre de Génétique Moléculaire · FRConsejo Superior de Investigaciones Científicas · ESInstituto de Biología Molecular y Celular de Plantas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA-binding protein phosphatases (DBPs) have been identified as a novel class of plant-specific regulatory factors playing a role in plant-virus interactions. NtDBP1 from tobacco (Nicotiana tabacum) was shown to participate in transcriptional regulation of gene expression in response to virus infection in compatible interactions, and AtDBP1, its closest relative in the model plant Arabidopsis (Arabidopsis thaliana), has recently been found to mediate susceptibility to potyvirus, one of the most speciose taxa of plant viruses. Here, we report on the identification of a novel family of highly conserved small polypeptides that interact with DBP1 proteins both in tobacco and Arabidopsis, which we have designated DBP-interacting protein 2 (DIP2). The interaction of AtDIP2 with AtDBP1 was demonstrated in vivo by bimolecular fluorescence complementation, and AtDIP2 was shown to functionally interfere with AtDBP1 in yeast. Furthermore, reducing AtDIP2 gene expression leads to increased susceptibility to the potyvirus Plum pox virus and to a lesser extent also to Turnip mosaic virus, whereas overexpression results in enhanced resistance. Therefore, we describe a novel family of conserved small polypeptides in plants and identify AtDIP2 as a novel host factor contributing to resistance to potyvirus in Arabidopsis.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsBase SequenceDNA-Binding ProteinsGene Expression Regulation, PlantHost-Pathogen InteractionsMolecular Sequence DataNicotianaPeptidesPhosphoprotein PhosphatasesPlant DiseasesPlant ImmunityPlant ProteinsPlum Pox VirusPotyvirusArabidopsis ProteinsDBP1 protein, ArabidopsisDNA-Binding ProteinsPeptidesPhosphoprotein PhosphatasesPlant ProteinsProtein Phosphatase 1Recombinant Fusion Proteins

Identifiers

PMID22021419
PMCPMC3327197
OpenAlexW2138095494

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.