Evidence map›Paper›PMID 35149763›Full record

ArticleCommunications biology2022

Structural and functional analyses explain Pea KAI2 receptor diversity and reveal stereoselective catalysis during signal perception.

Angelica M Guercio, Salar Torabi, David Cornu, Marion Dalmais, Abdelhafid Bendahmane, Christine Le Signor, Jean-Paul Pillot, Philippe Le Bris, François-Didier Boyer, Catherine Rameau and 3 more

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
6.5field-weighted citation impact, top 4% 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

19 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Mapping Strigolactone Hydrolysis in DWARF14 via QM/MM String Method.bioRxiv : the preprint server for biology · 2026
    Article
  4. Molecular insights into volatile organic compound sensing and signaling in plants.The Plant journal : for cell and molecular biology · 2026
    Review
  5. Review
  6. An N-terminal domain specifies developmental control by the SMAX1-LIKE family of transcriptional regulators inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. The Multifaceted Impact of Karrikin Signaling in Plants.International journal of molecular sciences · 2025
    Review
  8. Structural requirements of KAI2 ligands for activation of signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Strigolactones: diversity, perception, and hydrolysis.Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2023
    Article
  15. Review
  16. Article
  17. Article
  18. Crystal structure ofPlant direct · 2022
    Article
  19. 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

13 authors at 6 institutions in 3 countries.

Angelica M GuercioDepartment of Plant Biology, College of Biological Sciences, University of California, Davis, CA, 95616, USA.ORCID http://orcid.org/0000-0002-5464-1108
Salar TorabiPlant Genetics, TUM School of Life Sciences, Technical University of Munich (TUM), 85354, Freising, Germany.
David CornuUniversité Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198, Gif-sur-Yvette, France.
Marion DalmaisInstitute of Plant Sciences Paris-Saclay, INRAE, CNRS, Université Paris-Saclay, 91405, Orsay, France.
Abdelhafid BendahmaneInstitute of Plant Sciences Paris-Saclay, INRAE, CNRS, Université Paris-Saclay, 91405, Orsay, France.
Christine Le SignorAgroecologie, AgroSup Dijon, INRAE, Université Bourgogne Franche Comte, 21000, Dijon, France.
Jean-Paul PillotInstitut Jean-Pierre Bourgin, INRAE, AgroParisTech, Université Paris-Saclay, 78000, Versailles, France.
Philippe Le BrisInstitut Jean-Pierre Bourgin, INRAE, AgroParisTech, Université Paris-Saclay, 78000, Versailles, France.
François-Didier BoyerUniversité Paris-Saclay, CNRS, Institut de Chimie des Substances Naturelles, UPR 2301, 91198, Gif-sur-Yvette, France.ORCID http://orcid.org/0000-0001-9855-7234
Catherine RameauInstitut Jean-Pierre Bourgin, INRAE, AgroParisTech, Université Paris-Saclay, 78000, Versailles, France.
Caroline GutjahrPlant Genetics, TUM School of Life Sciences, Technical University of Munich (TUM), 85354, Freising, Germany.ORCID http://orcid.org/0000-0001-6163-745X
Alexandre de Saint GermainInstitut Jean-Pierre Bourgin, INRAE, AgroParisTech, Université Paris-Saclay, 78000, Versailles, France. Alexandre.De-Saint-Germain@inrae.fr.ORCID http://orcid.org/0000-0003-2814-7234
Nitzan ShabekDepartment of Plant Biology, College of Biological Sciences, University of California, Davis, CA, 95616, USA. nshabek@ucdavis.edu.ORCID http://orcid.org/0000-0002-2190-5955
AgroParisTech · FRCentre National de la Recherche Scientifique · FRTechnical University of Munich · DECarnegie Department of Plant Biology · USInstitut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRUniversity of California, Davis · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI PAUL David ADAMS, Gregory L Hura · 2017 to 2026
$28.6M
National Science Foundation (NSF) 2028283National Science Foundation (NSF) 2047396NIGMS NIH HHS P30 GM124169
6 · The paper itself

Abstract

KAI2 proteins are plant α/β hydrolase receptors which perceive smoke-derived butenolide signals and endogenous, yet unidentified KAI2-ligands (KLs). The number of functional KAI2 receptors varies among species and KAI2 gene duplication and sub-functionalization likely plays an adaptative role by altering specificity towards different KLs. Legumes represent one of the largest families of flowering plants and contain many agronomic crops. Prior to their diversification, KAI2 underwent duplication resulting in KAI2A and KAI2B. Here we demonstrate that Pisum sativum KAI2A and KAI2B are active receptors and enzymes with divergent ligand stereoselectivity. KAI2B has a higher affinity for and hydrolyses a broader range of substrates including strigolactone-like stereoisomers. We determine the crystal structures of PsKAI2B in apo and butenolide-bound states. The biochemical, structural, and mass spectra analyses of KAI2s reveal a transient intermediate on the catalytic serine and a stable adduct on the catalytic histidine, confirming its role as a bona fide enzyme. Our work uncovers the stereoselectivity of ligand perception and catalysis by diverged KAI2 receptors and proposes adaptive sensitivity to KAR/KL and strigolactones by KAI2B.

Indexed as

ArabidopsisArabidopsis ProteinsCatalysisPerceptionPisum sativumPlant Growth RegulatorsArabidopsis ProteinsPlant Growth Regulators

Identifiers

PMID35149763
PMCPMC8837635
OpenAlexW4220748874

What OpenQuestion holds

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LicenceCC BY
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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.