Evidence map›Paper›PMID 22270560›Full record

ArticlePlanta2012

ARAD proteins associated with pectic Arabinan biosynthesis form complexes when transiently overexpressed in planta.

Jesper Harholt, Jacob Krüger Jensen, Yves Verhertbruggen, Casper Søgaard, Sophie Bernard, Majse Nafisi, Christian Peter Poulsen, Naomi Geshi, Yumiko Sakuragi, Azeddine Driouich and 2 more

Abstract readComparative Study
PubMed Publisher
In one paragraph

Article in Planta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. A Pipeline towards the Biochemical Characterization of theInternational journal of molecular sciences · 2021
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. Separating Golgi Proteins fromThe Plant cell · 2019
    Article
  20. 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

12 authors.

Jesper HarholtLaboratory for Molecular Plant Biology, VKR Research Centre Pro-Active Plants, Department of Plant Biology and Biotechnology, University of Copenhagen, 1871, Frederiksberg C, Denmark.
Jacob Krüger Jensen
Yves Verhertbruggen
Casper Søgaard
Sophie Bernard
Majse Nafisi
Christian Peter Poulsen
Naomi Geshi
Yumiko Sakuragi
Azeddine Driouich
J Paul Knox
Henrik Vibe Scheller

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycosyltransferase complexes are known to be involved in plant cell wall biosynthesis, as for example in cellulose. It is not known to what extent such complexes are involved in biosynthesis of pectin as well. To address this question, work was initiated on ARAD1 (ARABINAN DEFICIENT 1) and its close homolog ARAD2 of glycosyltransferase family GT47. Using bimolecular fluorescence complementation, Förster resonance energy transfer and non-reducing gel electrophoresis, we show that ARAD1 and ARAD2 are localized in the same Golgi compartment and form homo-and heterodimeric intermolecular dimers when expressed transiently in Nicotiana benthamiana. Biochemical analysis of arad2 cell wall or fractions hereof showed no difference in the monosaccharide composition, when compared with wild type. The double mutant arad1 arad2 had an arad1 cell wall phenotype and overexpression of ARAD2 did not complement the arad1 phenotype, indicating that ARAD1 and ARAD2 are not redundant enzymes. To investigate the cell wall structure of the mutants in detail, immunohistochemical analyses were carried out on arad1, arad2 and arad1 arad2 using the arabinan-specific monoclonal antibody LM13. In roots, the labeling pattern of arad2 was distinct from both that of wild type, arad1 and arad1 arad2. Likewise, in epidermal cell walls of inflorescence stems, LM13 binding differed between arad2 and WILD TYPE, arad1 or arad1 arad2. Altogether, these data show that ARAD2 is associated with arabinan biosynthesis, not redundant with ARAD1, and that the two glycosyltransferases may function in complexes held together by disulfide bridges.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCell WallDisulfidesGene Expression Regulation, EnzymologicGene Expression Regulation, PlantGenes, PlantGenetic VariationGenotypeGlycosyltransferasesMutationNicotianaPectinsPentosyltransferasesPlant Growth RegulatorsarabanArabidopsis ProteinsARAD2 protein, ArabidopsisDisulfidesGlycosyltransferasesPectinsPentosyltransferasesPlant Growth RegulatorsPolysaccharides

Identifiers

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Read underepoch 390

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.