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.

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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.

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  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

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