Evidence map›Paper›PMID 25352273›Full record

ArticlePlant physiology2014

Catalytic subunit stoichiometry within the cellulose synthase complex.

Martine Gonneau, Thierry Desprez, Alain Guillot, Samantha Vernhettes, Herman Höfte

Abstract read
In one paragraph

Article in Plant physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed.

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  15. Structure ofProceedings of the National Academy of Sciences of the United States of America · 2021
    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

5 authors.

Martine GonneauInstitut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, F-78000 Versailles, France (M.G., T.D., S.V., H.H.);AgroParisTech, Institut Jean-Pierre Bourgin, F-78000 Versailles, France (M.G., T.D., S.V., H.H.); andInstitut National de la Recherche Agronomique, Unité Mixte de Recherche, Microbiologie de l'Alimentation au Service de la Santé, Plateforme d'Analyse Protéomique de Paris Sud-Ouest, Domaine de Vilvert 78352, Jouy en Josas cedex, France (A.G.) martine.gonneau@versailles.inra.fr.
Thierry DesprezInstitut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, F-78000 Versailles, France (M.G., T.D., S.V., H.H.);AgroParisTech, Institut Jean-Pierre Bourgin, F-78000 Versailles, France (M.G., T.D., S.V., H.H.); andInstitut National de la Recherche Agronomique, Unité Mixte de Recherche, Microbiologie de l'Alimentation au Service de la Santé, Plateforme d'Analyse Protéomique de Paris Sud-Ouest, Domaine de Vilvert 78352, Jouy en Josas cedex, France (A.G.).
Alain GuillotInstitut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, F-78000 Versailles, France (M.G., T.D., S.V., H.H.);AgroParisTech, Institut Jean-Pierre Bourgin, F-78000 Versailles, France (M.G., T.D., S.V., H.H.); andInstitut National de la Recherche Agronomique, Unité Mixte de Recherche, Microbiologie de l'Alimentation au Service de la Santé, Plateforme d'Analyse Protéomique de Paris Sud-Ouest, Domaine de Vilvert 78352, Jouy en Josas cedex, France (A.G.).
Samantha VernhettesInstitut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, F-78000 Versailles, France (M.G., T.D., S.V., H.H.);AgroParisTech, Institut Jean-Pierre Bourgin, F-78000 Versailles, France (M.G., T.D., S.V., H.H.); andInstitut National de la Recherche Agronomique, Unité Mixte de Recherche, Microbiologie de l'Alimentation au Service de la Santé, Plateforme d'Analyse Protéomique de Paris Sud-Ouest, Domaine de Vilvert 78352, Jouy en Josas cedex, France (A.G.).
Herman HöfteInstitut National de la Recherche Agronomique, Unité Mixte de Recherche 1318, Institut Jean-Pierre Bourgin, Saclay Plant Sciences, F-78000 Versailles, France (M.G., T.D., S.V., H.H.);AgroParisTech, Institut Jean-Pierre Bourgin, F-78000 Versailles, France (M.G., T.D., S.V., H.H.); andInstitut National de la Recherche Agronomique, Unité Mixte de Recherche, Microbiologie de l'Alimentation au Service de la Santé, Plateforme d'Analyse Protéomique de Paris Sud-Ouest, Domaine de Vilvert 78352, Jouy en Josas cedex, France (A.G.).

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellulose synthesis is driven by large plasma membrane-inserted protein complexes, which in plants have 6-fold symmetry. In Arabidopsis (Arabidopsis thaliana), functional cellulose synthesis complexes (CSCs) are composed of at least three different cellulose synthase catalytic subunits (CESAs), but the actual ratio of the CESA isoforms within the CSCs remains unresolved. In this work, the stoichiometry of the CESAs in the primary cell wall CSC was determined, after elimination of CESA redundancy in a mutant background, by coimmunoprecipitation and mass spectrometry using label-free quantitative methods. Based on spectral counting, we show that CESA1, CESA3, and CESA6 are present in a 1:1:1 molecular ratio.

Indexed as

ArabidopsisArabidopsis ProteinsCatalytic DomainCell WallGlucosyltransferasesImmunoprecipitationIsoenzymesMass SpectrometryMembrane ProteinsProteomicsSeedlingsArabidopsis ProteinsAt5g05170 protein, ArabidopsisCESA1 protein, ArabidopsisGlucosyltransferasesIsoenzymesMembrane ProteinsPRC1 protein, Arabidopsis

Identifiers

PMID25352273
PMCPMC4256875

What OpenQuestion holds

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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.