Evidence map›Paper›PMID 34651644›Full record

ArticleJournal of experimental botany2022

Arabidopsis fibrillin 1-2 subfamily members exert their functions via specific protein-protein interactions.

Diego Torres-Romero, Ángeles Gómez-Zambrano, Antonio Jesús Serrato, Mariam Sahrawy, Ángel Mérida

Open access · hybridAbstract read
In one paragraph

Article in Journal of experimental botany, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

17 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  8. Plants (Basel, Switzerland) · 2024
    Article
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  11. Redox dynamics in seeds ofFrontiers in plant science · 2024
    Article
  12. Review
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  14. Article
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  17. 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

5 authors at 2 institutions in 1 country.

Diego Torres-RomeroInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas (CSIC) - Universidad de Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain.
Ángeles Gómez-ZambranoInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas (CSIC) - Universidad de Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain.
Antonio Jesús SerratoEstación Experimental del Zaidín, CSIC, Calle Profesor Albareda 1, 18008 Granada, Spain.
Mariam SahrawyEstación Experimental del Zaidín, CSIC, Calle Profesor Albareda 1, 18008 Granada, Spain.
Ángel MéridaInstituto de Bioquímica Vegetal y Fotosíntesis, Consejo Superior de Investigaciones Científicas (CSIC) - Universidad de Sevilla, Avenida Américo Vespucio 49, 41092 Sevilla, Spain.ORCID 0000-0002-0880-2329
Consejo Superior de Investigaciones Científicas · ESEstación Experimental del Zaidín · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fibrillins (FBNs) are plastidial proteins found in photosynthetic organisms from cyanobacteria to higher plants. The function of most FBNs remains unknown. Here, we focused on members of the FBN subgroup comprising FBN1a, FBN1b, and FBN2. We show that these three polypeptides interact between each other, potentially forming a network around the plastoglobule surface. Both FBN2 and FBN1s interact with allene oxide synthase, and the elimination of any of these FBNs results in a delay in jasmonate-mediated anthocyanin accumulation in response to a combination of moderate high light and low temperature. Mutations in the genes encoding FBN1s or FBN2 also affect the protection of PSII under the combination of these stresses. Fully developed leaves of these mutants have lower maximum quantum efficiency of PSII (Fv/Fm) and higher oxidative stress than wild-type plants. These effects are additive, and the fbn1a-1b-2 triple mutant shows a stronger decrease in Fv/Fm and a greater increase in oxidative stress than fbn1a-1b or fbn2 mutants. Co-immunoprecipitation analysis indicated that FBN2 also interacts with other proteins involved in different metabolic processes. We propose that these fibrillins facilitate accurate positioning of different proteins involved in distinct metabolic processes, and that their elimination leads to dysfunction of those proteins.

Indexed as

ArabidopsisArabidopsis ProteinsChloroplastsFibrillin-1FibrillinsArabidopsis ProteinsFibrillin-1FibrillinsAbiotic stressArabidopsisfibrillinjasmonatephotosystem IIplastoglobule

Identifiers

PMID34651644
PMCPMC8793873
OpenAlexW3207713430

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.