Evidence map›Paper›PMID 38049516›Full record

ArticleNature plants2023

Subtilase-mediated biogenesis of the expanded family of SERINE RICH ENDOGENOUS PEPTIDES.

Huanjie Yang, Xeniya Kim, Jan Skłenar, Sébastien Aubourg, Gloria Sancho-Andrés, Elia Stahl, Marie-Charlotte Guillou, Nora Gigli-Bisceglia, Loup Tran Van Canh, Kyle W Bender and 9 more

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In one paragraph

Article in Nature plants, 2023. 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
9.4field-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

42 citing papers in PubMed, 51 citations in OpenAlex.

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  13. Processing and release of endogenous immunogenic peptide signals.The Plant journal : for cell and molecular biology · 2026
    Review
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  15. Plant subtilases as key initiators of peptide ligand-receptor signaling.The Plant journal : for cell and molecular biology · 2026
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors at 9 institutions in 7 countries.

Huanjie YangInstitute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland.
Xeniya KimInstitute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland.
Jan SkłenarThe Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.ORCID http://orcid.org/0000-0003-1858-2574
Sébastien AubourgUniversité Angers, Institut Agro, INRAE, IRHS, SFR QUASAV, Angers, France.ORCID http://orcid.org/0000-0002-0695-4767
Gloria Sancho-AndrésInstitute of Molecular Plant Biology, ETH Zurich, Zurich, Switzerland.
Elia StahlDepartment of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland.
Marie-Charlotte GuillouUniversité Angers, Institut Agro, INRAE, IRHS, SFR QUASAV, Angers, France.
Nora Gigli-BiscegliaLaboratory of Plant Physiology, Wageningen University and Research, Wageningen, the Netherlands.ORCID http://orcid.org/0000-0002-6907-1427
Loup Tran Van CanhUniversité Angers, Institut Agro, INRAE, IRHS, SFR QUASAV, Angers, France.
Kyle W BenderInstitute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland.
Annick StintziInstitute of Biology, Plant Physiology and Biochemistry, University of Hohenheim, Stuttgart, Germany.ORCID http://orcid.org/0000-0002-6479-8184
Philippe ReymondDepartment of Plant Molecular Biology, University of Lausanne, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-3341-6200
Clara Sánchez-RodríguezInstitute of Molecular Plant Biology, ETH Zurich, Zurich, Switzerland.
Christa TesterinkLaboratory of Plant Physiology, Wageningen University and Research, Wageningen, the Netherlands.ORCID http://orcid.org/0000-0001-6738-115X
Jean-Pierre RenouUniversité Angers, Institut Agro, INRAE, IRHS, SFR QUASAV, Angers, France.
Frank L H MenkeThe Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK.ORCID http://orcid.org/0000-0003-2490-4824
Andreas SchallerInstitute of Biology, Plant Physiology and Biochemistry, University of Hohenheim, Stuttgart, Germany.ORCID http://orcid.org/0000-0001-6872-9576
Jack RhodesThe Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich, UK. jack.rhodes@tsl.ac.uk.ORCID http://orcid.org/0000-0002-3953-1648
Cyril ZipfelInstitute of Plant and Microbial Biology, Zurich-Basel Plant Science Center, University of Zurich, Zurich, Switzerland. cyril.zipfel@botinst.uzh.ch.ORCID http://orcid.org/0000-0003-4935-8583
Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement · FRUniversity of East Anglia · GBETH Zurich · CHUniversity of Hohenheim · DEUniversity of Lausanne · CHUniversity of Zurich · CHChinese Academy of Sciences · CNUtrecht University · NLWageningen University & Research · NL

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 724321EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 773153Gatsby Charitable Foundation n/aRCUK | Biotechnology and Biological Sciences Research Council (BBSRC) BB/P012574/1Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 310030_184769Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (Swiss National Science Foundation) 31003A_182625
6 · The paper itself

Abstract

Plant signalling peptides are typically released from larger precursors by proteolytic cleavage to regulate plant growth, development and stress responses. Recent studies reported the characterization of a divergent family of Brassicaceae-specific peptides, SERINE RICH ENDOGENOUS PEPTIDES (SCOOPs), and their perception by the leucine-rich repeat receptor kinase MALE DISCOVERER 1-INTERACTING RECEPTOR-LIKE KINASE 2 (MIK2). Here, we reveal that the SCOOP family is highly expanded, containing at least 50 members in the Columbia-0 reference Arabidopsis thaliana genome. Notably, perception of these peptides is strictly MIK2-dependent. How bioactive SCOOP peptides are produced, and to what extent their perception is responsible for the multiple physiological roles associated with MIK2 are currently unclear. Using N-terminomics, we validate the N-terminal cleavage site of representative PROSCOOPs. The cleavage sites are determined by conserved motifs upstream of the minimal SCOOP bioactive epitope. We identified subtilases necessary and sufficient to process PROSCOOP peptides at conserved cleavage motifs. Mutation of these subtilases, or their recognition motifs, suppressed PROSCOOP cleavage and associated overexpression phenotypes. Furthermore, we show that higher-order mutants of these subtilases show phenotypes reminiscent of mik2 null mutant plants, consistent with impaired PROSCOOP biogenesis, and demonstrating biological relevance of SCOOP perception by MIK2. Together, this work provides insights into the molecular mechanisms underlying the functions of the recently identified SCOOP peptides and their receptor MIK2.

Indexed as

ArabidopsisArabidopsis ProteinsBrassicaceaePeptidesProtein KinasesReceptors, Cell SurfaceSerineArabidopsis ProteinsMIK2 protein, ArabidopsisPeptidesProtein KinasesReceptors, Cell SurfaceSerine

Identifiers

PMID38049516
OpenAlexW4389304790

What OpenQuestion holds

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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.