Evidence map›Paper›PMID 27058169›Full record

ArticleeLife2016

Mechanistic insight into a peptide hormone signaling complex mediating floral organ abscission.

Julia Santiago, Benjamin Brandt, Mari Wildhagen, Ulrich Hohmann, Ludwig A Hothorn, Melinka A Butenko, Michael Hothorn

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed
15.3field-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

117 citing papers in PubMed, 263 citations in OpenAlex.

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  12. Plant subtilases as key initiators of peptide ligand-receptor signaling.The Plant journal : for cell and molecular biology · 2026
    Review
  13. Article
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  15. Review
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  17. Review
  18. Advances of Peptides for Plant Immunity.Plants (Basel, Switzerland) · 2025
    Review
  19. Article
  20. Article

57 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

7 authors at 3 institutions in 3 countries.

Julia SantiagoStructural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
Benjamin BrandtStructural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
Mari WildhagenDepartment of Biosciences, Section for Genetic and Evolutionary Biology, University of Oslo, Oslo, Norway.
Ulrich HohmannStructural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.
Ludwig A HothornInstitute of Biostatistics, Leibniz University, Hannover, Germany.
Melinka A ButenkoDepartment of Biosciences, Section for Genetic and Evolutionary Biology, University of Oslo, Oslo, Norway.
Michael HothornStructural Plant Biology Laboratory, Department of Botany and Plant Biology, University of Geneva, Geneva, Switzerland.ORCID 0000-0002-3597-5698
University of Geneva · CHUniversity of Oslo · NOLeibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plants constantly renew during their life cycle and thus require to shed senescent and damaged organs. Floral abscission is controlled by the leucine-rich repeat receptor kinase (LRR-RK) HAESA and the peptide hormone IDA. It is unknown how expression of IDA in the abscission zone leads to HAESA activation. Here we show that IDA is sensed directly by the HAESA ectodomain. Crystal structures of HAESA in complex with IDA reveal a hormone binding pocket that accommodates an active dodecamer peptide. A central hydroxyproline residue anchors IDA to the receptor. The HAESA co-receptor SERK1, a positive regulator of the floral abscission pathway, allows for high-affinity sensing of the peptide hormone by binding to an Arg-His-Asn motif in IDA. This sequence pattern is conserved among diverse plant peptides, suggesting that plant peptide hormone receptors may share a common ligand binding mode and activation mechanism.

Indexed as

Gene Expression Regulation, PlantSignal TransductionArabidopsisArabidopsis ProteinsBinding SitesCrystallography, X-RayFlowersProtein BindingProtein ConformationProtein KinasesProtein Serine-Threonine KinasesArabidopsis ProteinsIDA protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesRLK5 protein, ArabidopsisSERK1 protein, Arabidopsisbiophysicsfloral abscission<i>a. thaliana</i>membrane signalingpeptide hormoneplant biologyplant developmentprotein complexesreceptor kinasestructural biology

Identifiers

PMID27058169
PMCPMC4848090
OpenAlexW2315721191

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.