Evidence map›Paper›PMID 22327741›Full record

ArticleThe Plant cell2012

Chitinase-like1/pom-pom1 and its homolog CTL2 are glucan-interacting proteins important for cellulose biosynthesis in Arabidopsis.

Clara Sánchez-Rodríguez, Stefan Bauer, Kian Hématy, Friederike Saxe, Ana Belén Ibáñez, Vera Vodermaier, Cornelia Konlechner, Arun Sampathkumar, Markus Rüggeberg, Ernst Aichinger and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
19.3field-weighted citation impact, top 1% 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

80 citing papers in PubMed, 174 citations in OpenAlex.

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  17. Building an extensible cell wall.Plant physiology · 2022
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20 more citing papers are in PubMed but not listed here.

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

15 authors at 7 institutions in 4 countries.

Clara Sánchez-RodríguezMax-Planck-Institut für Molekulare Pflanzenphysiologie, 14476 Potsdam-Golm, Germany.
Stefan Bauer
Kian Hématy
Friederike Saxe
Ana Belén Ibáñez
Vera Vodermaier
Cornelia Konlechner
Arun Sampathkumar
Markus Rüggeberg
Ernst Aichinger
Lutz Neumetzler
Ingo Burgert
Chris Somerville
Marie-Theres Hauser
Staffan Persson
BOKU University · ATMax Planck Institute of Molecular Plant Physiology · DEEnergy Biosciences Institute · USÉcole Polytechnique Fédérale de Lausanne · CHMax Planck Institute of Colloids and Interfaces · DESwiss Federal Laboratories for Materials Science and Technology · CHUniversity of California, Berkeley · US

Funding

Austrian Science Fund FWF I 1725
6 · The paper itself

Abstract

Plant cells are encased by a cellulose-containing wall that is essential for plant morphogenesis. Cellulose consists of β-1,4-linked glucan chains assembled into paracrystalline microfibrils that are synthesized by plasma membrane-located cellulose synthase (CESA) complexes. Associations with hemicelluloses are important for microfibril spacing and for maintaining cell wall tensile strength. Several components associated with cellulose synthesis have been identified; however, the biological functions for many of them remain elusive. We show that the chitinase-like (CTL) proteins, CTL1/POM1 and CTL2, are functionally equivalent, affect cellulose biosynthesis, and are likely to play a key role in establishing interactions between cellulose microfibrils and hemicelluloses. CTL1/POM1 coincided with CESAs in the endomembrane system and was secreted to the apoplast. The movement of CESAs was compromised in ctl1/pom1 mutant seedlings, and the cellulose content and xyloglucan structures were altered. X-ray analysis revealed reduced crystalline cellulose content in ctl1 ctl2 double mutants, suggesting that the CTLs cooperatively affect assembly of the glucan chains, which may affect interactions between hemicelluloses and cellulose. Consistent with this hypothesis, both CTLs bound glucan-based polymers in vitro. We propose that the apoplastic CTLs regulate cellulose assembly and interaction with hemicelluloses via binding to emerging cellulose microfibrils.

Indexed as

ArabidopsisArabidopsis ProteinsCelluloseCell WallChitinasesGlucansGlycoside HydrolasesMicrofibrilsPlants, Genetically ModifiedPolysaccharidesArabidopsis ProteinsCelluloseChitinasesCTL1 protein, ArabidopsisGlucansGlycoside HydrolaseshemicellulosePolysaccharides

Identifiers

PMID22327741
PMCPMC3315235
OpenAlexW2158850705

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.