Evidence map›Paper›PMID 25340959›Full record

ArticleeLife2014

The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1.

Yangrong Cao, Yan Liang, Kiwamu Tanaka, Cuong T Nguyen, Robert P Jedrzejczak, Andrzej Joachimiak, Gary Stacey

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 301 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
301citing papers in PubMed, 1 pooled it
54.1field-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

301 citing papers in PubMed, 1 synthesis or guideline pooled it, 674 citations in OpenAlex.

  1. Pooled it
  2. Chitosan activates a sequential CaPlant signaling & behavior · 2026
    Article
  3. Mechanisms and balanced regulation of plant immunity.Nature reviews. Molecular cell biology · 2026
    Review
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241 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 2 institutions in 1 country.

Yangrong CaoDivision of Plant Sciences, National Center for Soybean Biotechnology, University of Missouri, Columbia, United States.
Yan LiangDivision of Plant Sciences, National Center for Soybean Biotechnology, University of Missouri, Columbia, United States.
Kiwamu TanakaDivision of Plant Sciences, National Center for Soybean Biotechnology, University of Missouri, Columbia, United States.ORCID http://orcid.org/0000-0001-5045-560X
Cuong T NguyenDivision of Plant Sciences, National Center for Soybean Biotechnology, University of Missouri, Columbia, United States.
Robert P JedrzejczakMidwest Center for Structural Genomics, Argonne National Laboratory, Argonne, United States.
Andrzej JoachimiakMidwest Center for Structural Genomics, Argonne National Laboratory, Argonne, United States.
Gary StaceyDivision of Plant Sciences, National Center for Soybean Biotechnology, University of Missouri, Columbia, United States.
University of Missouri · USArgonne National Laboratory · US

Funding

Midwest Center for Structural GenomicsU54GM094585 · NIGMS · UNIVERSITY OF CHICAGO · PI MINOR, WLADEK · 2010 to 2014
$33.7M
NIGMS NIH HHS GM094585NIGMS NIH HHS U54 GM094585
6 · The paper itself

Abstract

Chitin is a fungal microbe-associated molecular pattern recognized in Arabidopsis by a lysin motif receptor kinase (LYK), AtCERK1. Previous research suggested that AtCERK1 is the major chitin receptor and mediates chitin-induced signaling through homodimerization and phosphorylation. However, the reported chitin binding affinity of AtCERK1 is quite low, suggesting another receptor with high chitin binding affinity might be present. Here, we propose that AtLYK5 is the primary chitin receptor in Arabidopsis. Mutations in AtLYK5 resulted in a significant reduction in chitin response. However, AtLYK5 shares overlapping function with AtLYK4 and, therefore, Atlyk4/Atlyk5-2 double mutants show a complete loss of chitin response. AtLYK5 interacts with AtCERK1 in a chitin-dependent manner. Chitin binding to AtLYK5 is indispensable for chitin-induced AtCERK1 phosphorylation. AtLYK5 binds chitin at a much higher affinity than AtCERK1. The data suggest that AtLYK5 is the primary receptor for chitin, forming a chitin inducible complex with AtCERK1 to induce plant immunity.

Indexed as

ArabidopsisArabidopsis ProteinsChitinModels, MolecularMutationPhosphorylationPlant ImmunityProtein BindingProtein KinasesProtein MultimerizationProtein Serine-Threonine KinasesProtein Structure, TertiaryReceptors, Cell SurfaceSerineSignal TransductionTyrosineArabidopsis ProteinsCERK1 protein, ArabidopsisChitinLYK5 protein, ArabidopsisProtein KinasesProtein Serine-Threonine KinasesReceptors, Cell SurfaceSerineTyrosineArabidoposisarabidopsisCERK1chitin receptorLYK5plant biologyplant innate immunity

Identifiers

PMID25340959
PMCPMC4356144
OpenAlexW2125627131

What OpenQuestion holds

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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.