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

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          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.

          DOI: http://dx.doi.org/10.7554/eLife.03766.001

          eLife digest

          Invading fungi are responsible for many of the plant diseases that affect global crop production. Plants have to be able to identify these fungi, and activate the right defense strategies if they are to protect themselves. Chitin is a polymer that is found in the cell walls of all fungi, but not in plants, so if the plant detects chitin, it knows that a potentially harmful fungus may be nearby.

          The detection of chitin, and the resulting activation of a plant's defenses, requires a receptor protein called CERK1. In rice, CERK1 needs to interact with another receptor protein called CEBiP, which binds to chitin. However, in Arabidopsis thaliana—which is widely studied in plant research—CERK1 can bind to chitin on its own, although this interaction is very weak, so it has been suggested that a second protein may be involved.

          Cao et al. have now found that a receptor protein called LYK5, which is very similar to CERK1, is much better at attaching to chitin in A. thaliana. It can also bind to CERK1, but only when chitin is present, and is required for activation of basic plant defenses. The experiments suggest that LYK5 detects chitin on behalf of CERK1, in a similar way to how CEBiP works in rice.

          The next step in this research is to work out how CERK1 and LYK5 are able to activate plant defenses.

          DOI: http://dx.doi.org/10.7554/eLife.03766.002

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          Most cited references71

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                Author and article information

                Contributors
                Role: Reviewing editor
                Journal
                eLife
                eLife
                eLife
                eLife
                eLife Sciences Publications, Ltd
                2050-084X
                2050-084X
                23 October 2014
                2014
                : 3
                : e03766
                Affiliations
                [1]deptDivision of Plant Sciences, National Center for Soybean Biotechnology , University of Missouri , Columbia, United States
                [2]deptDepartment of Biochemistry , University of Missouri , Columbia, United States
                [3]deptMidwest Center for Structural Genomics , Argonne National Laboratory , Argonne, United States
                Tübingen University , Germany
                Tübingen University , Germany
                Author notes
                [* ]For correspondence: Staceyg@ 123456missouri.edu
                [†]

                These authors contributed equally to this work.

                [‡]

                Department of Plant Pathology, Washington State University, Pullman, United States.

                Author information
                http://orcid.org/0000-0001-5045-560X
                Article
                03766
                10.7554/eLife.03766
                4356144
                25340959
                9c4e4be5-f189-4822-8f90-9b9194498f3e

                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.

                History
                : 27 June 2014
                : 22 October 2014
                Funding
                Funded by: FundRef http://dx.doi.org/10.13039/501100003627, Rural Development Administration;
                Award ID: Next-Generation BioGreen 21 Program Systems and Synthetic Agrobiotech CenterPJ009068
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/100006151, Basic Energy Sciences;
                Award ID: DE-FG02-08ER15309
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/100006206, Biological and Environmental Research;
                Award ID: DE-AC02-06CH11357
                Award Recipient :
                Funded by: FundRef http://dx.doi.org/10.13039/100000002, National Institutes of Health;
                Award ID: GM094585
                Award Recipient :
                The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
                Categories
                Research Article
                Plant Biology
                Custom metadata
                2
                The chitin-triggered immune response is mediated by a LYK5 and CERK1 receptor complex in Arabidopsis.

                Life sciences
                arabidoposis,plant innate immunity,chitin receptor,cerk1,lyk5,arabidopsis
                Life sciences
                arabidoposis, plant innate immunity, chitin receptor, cerk1, lyk5, arabidopsis

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