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

  1. Yangrong Cao
  2. Yan Liang
  3. Kiwamu Tanaka
  4. Cuong T Nguyen
  5. Robert P Jedrzejczak
  6. Andrzej Joachimiak
  7. Gary Stacey  Is a corresponding author
  1. University of Missouri, United States
  2. Washington State University, United States
  3. Argonne National Laboratory, United States

Abstract

Chitin is a fungal microbe-associated molecular pattern (MAMP) that is recognized in Arabidopsis by a lysin motif receptor kinase (LYK), AtCERK1. Previous research suggested that AtCERK1 is the major chitin receptor in plants 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 the plant chitin response. However, AtLYK5 shares overlapping function with AtLYK4 and, therefore, only 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 higher affinity than AtCERK1. The data suggest that AtLYK5 is the primary receptor for chitin to induce plant immunity.

Article and author information

Author details

  1. Yangrong Cao

    University of Missouri, Columbia, United States
    Competing interests
    The authors declare that no competing interests exist.
  2. Yan Liang

    University of Missouri, Columbia, United States
    Competing interests
    The authors declare that no competing interests exist.
  3. Kiwamu Tanaka

    Washington State University, Pullman, United States
    Competing interests
    The authors declare that no competing interests exist.
  4. Cuong T Nguyen

    University of Missouri, Columbia, United States
    Competing interests
    The authors declare that no competing interests exist.
  5. Robert P Jedrzejczak

    Argonne National Laboratory, Argonne, United States
    Competing interests
    The authors declare that no competing interests exist.
  6. Andrzej Joachimiak

    Argonne National Laboratory, Argonne, United States
    Competing interests
    The authors declare that no competing interests exist.
  7. Gary Stacey

    University of Missouri, Columbia, United States
    For correspondence
    Staceyg@missouri.edu
    Competing interests
    The authors declare that no competing interests exist.

Reviewing Editor

  1. Thorsten Nürnberger, Tübingen University, Germany

Version history

  1. Received: June 27, 2014
  2. Accepted: October 22, 2014
  3. Accepted Manuscript published: October 23, 2014 (version 1)
  4. Version of Record published: November 12, 2014 (version 2)

Copyright

This is an open-access article, free of all copyright, and may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose. The work is made available under the Creative Commons CC0 public domain dedication.

Metrics

  • 9,984
    Page views
  • 1,957
    Downloads
  • 420
    Citations

Article citation count generated by polling the highest count across the following sources: Scopus, Crossref, PubMed Central.

Download links

A two-part list of links to download the article, or parts of the article, in various formats.

Downloads (link to download the article as PDF)

Open citations (links to open the citations from this article in various online reference manager services)

Cite this article (links to download the citations from this article in formats compatible with various reference manager tools)

  1. Yangrong Cao
  2. Yan Liang
  3. Kiwamu Tanaka
  4. Cuong T Nguyen
  5. Robert P Jedrzejczak
  6. Andrzej Joachimiak
  7. Gary Stacey
(2014)
The kinase LYK5 is a major chitin receptor in Arabidopsis and forms a chitin-induced complex with related kinase CERK1
eLife 3:e03766.
https://doi.org/10.7554/eLife.03766

Share this article

https://doi.org/10.7554/eLife.03766

Further reading

    1. Plant Biology
    Daniel S Yu, Megan A Outram ... Simon J Williams
    Research Article

    Plant pathogens secrete proteins, known as effectors, that function in the apoplast or inside plant cells to promote virulence. Effector recognition by cell-surface or cytosolic receptors results in the activation of defence pathways and plant immunity. Despite their importance, our general understanding of fungal effector function and recognition by immunity receptors remains poor. One complication often associated with effectors is their high sequence diversity and lack of identifiable sequence motifs precluding prediction of structure or function. In recent years, several studies have demonstrated that fungal effectors can be grouped into structural classes, despite significant sequence variation and existence across taxonomic groups. Using protein X-ray crystallography, we identify a new structural class of effectors hidden within the secreted in xylem (SIX) effectors from Fusarium oxysporum f. sp. lycopersici (Fol). The recognised effectors Avr1 (SIX4) and Avr3 (SIX1) represent the founding members of the Fol dual-domain (FOLD) effector class, with members containing two distinct domains. Using AlphaFold2, we predicted the full SIX effector repertoire of Fol and show that SIX6 and SIX13 are also FOLD effectors, which we validated experimentally for SIX6. Based on structural prediction and comparisons, we show that FOLD effectors are present within three divisions of fungi and are expanded in pathogens and symbionts. Further structural comparisons demonstrate that Fol secretes effectors that adopt a limited number of structural folds during infection of tomato. This analysis also revealed a structural relationship between transcriptionally co-regulated effector pairs. We make use of the Avr1 structure to understand its recognition by the I receptor, which leads to disease resistance in tomato. This study represents an important advance in our understanding of Fol-tomato, and by extension plant–fungal interactions, which will assist in the development of novel control and engineering strategies to combat plant pathogens.

    1. Ecology
    2. Plant Biology
    Jamie Mitchel Waterman, Tristan Michael Cofer ... Matthias Erb
    Research Article

    Volatiles emitted by herbivore-attacked plants (senders) can enhance defenses in neighboring plants (receivers), however, the temporal dynamics of this phenomenon remain poorly studied. Using a custom-built, high-throughput proton transfer reaction time-of-flight mass spectrometry (PTR-ToF-MS) system, we explored temporal patterns of volatile transfer and responses between herbivore-attacked and undamaged maize plants. We found that continuous exposure to natural blends of herbivore-induced volatiles results in clocked temporal response patterns in neighboring plants, characterized by an induced terpene burst at the onset of the second day of exposure. This delayed burst is not explained by terpene accumulation during the night, but coincides with delayed jasmonate accumulation in receiver plants. The delayed burst occurs independent of day:night light transitions and cannot be fully explained by sender volatile dynamics. Instead, it is the result of a stress memory from volatile exposure during the first day and secondary exposure to bioactive volatiles on the second day. Our study reveals that prolonged exposure to natural blends of stress-induced volatiles results in a response that integrates priming and direct induction into a distinct and predictable temporal response pattern. This provides an answer to the long-standing question of whether stress volatiles predominantly induce or prime plant defenses in neighboring plants, by revealing that they can do both in sequence.