Evidence map›Paper›PMID 23175744›Full record

ArticleThe Plant cell2012

Protein-protein and protein-membrane associations in the lignin pathway.

Jean-Etienne Bassard, Ludovic Richert, Jan Geerinck, Hugues Renault, Frédéric Duval, Pascaline Ullmann, Martine Schmitt, Etienne Meyer, Jerôme Mutterer, Wout Boerjan and 4 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 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

74 citing papers in PubMed, 145 citations in OpenAlex.

  1. Article
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  6. Review
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  8. Article
  9. Review
  10. Article
  11. Immunoprecipitation and FRET-FLIM to Determine Metabolons on the Plant ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  12. Article
  13. Raspberry Ketone Accumulation inJournal of agricultural and food chemistry · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Cloning and Characterization of Two NovelInternational journal of molecular sciences · 2022
    Article
  18. Article
  19. Review
  20. Interactome of Arabidopsis Thaliana.Plants (Basel, Switzerland) · 2022
    Article

14 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

14 authors at 5 institutions in 2 countries.

Jean-Etienne BassardInstitute of Plant Molecular Biology of Centre National de la Recherche Scientifique, Unité Propre de Recherche 2357, University of Strasbourg, F-67000 Strasbourg, France.
Ludovic Richert
Jan Geerinck
Hugues Renault
Frédéric Duval
Pascaline Ullmann
Martine Schmitt
Etienne Meyer
Jerôme Mutterer
Wout Boerjan
Geert De Jaeger
Yves Mely
Alain Goossens
Danièle Werck-Reichhart
Centre National de la Recherche Scientifique · FRGhent University · BEUniversité de Strasbourg · FRLaboratoire d'Innovation Thérapeutique · FRVlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Supramolecular organization of enzymes is proposed to orchestrate metabolic complexity and help channel intermediates in different pathways. Phenylpropanoid metabolism has to direct up to 30% of the carbon fixed by plants to the biosynthesis of lignin precursors. Effective coupling of the enzymes in the pathway thus seems to be required. Subcellular localization, mobility, protein-protein, and protein-membrane interactions of four consecutive enzymes around the main branch point leading to lignin precursors was investigated in leaf tissues of Nicotiana benthamiana and cells of Arabidopsis thaliana. CYP73A5 and CYP98A3, the two Arabidopsis cytochrome P450s (P450s) catalyzing para- and meta-hydroxylations of the phenolic ring of monolignols were found to colocalize in the endoplasmic reticulum (ER) and to form homo- and heteromers. They moved along with the fast remodeling plant ER, but their lateral diffusion on the ER surface was restricted, likely due to association with other ER proteins. The connecting soluble enzyme hydroxycinnamoyltransferase (HCT), was found partially associated with the ER. Both HCT and the 4-coumaroyl-CoA ligase relocalized closer to the membrane upon P450 expression. Fluorescence lifetime imaging microscopy supports P450 colocalization and interaction with the soluble proteins, enhanced by the expression of the partner proteins. Protein relocalization was further enhanced in tissues undergoing wound repair. CYP98A3 was the most effective in driving protein association.

Indexed as

Acyl Coenzyme AAcyltransferasesArabidopsisArabidopsis ProteinsCoenzyme A LigasesCytochrome P-450 Enzyme SystemEndoplasmic ReticulumGreen Fluorescent ProteinsHydroxybenzoatesHydroxylationLigninMembrane ProteinsNicotianaPlant LeavesPlants, Genetically ModifiedProtein Interaction Mapping4-coumaroyl-coenzyme AAcyl Coenzyme AAcyltransferasesArabidopsis ProteinsCoenzyme A LigasesCYP73A5 protein, ArabidopsisCYP98A3 protein, ArabidopsisCytochrome P-450 Enzyme Systemenhanced green fluorescent proteinGreen Fluorescent ProteinsHydroxybenzoatesLigninMembrane Proteinsphenolic acidRecombinant Fusion ProteinsTrans-Cinnamate 4-Monooxygenase

Identifiers

PMID23175744
PMCPMC3531846
OpenAlexW2148428417

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.