Arabidopsis CPK5 Phosphorylates the Chitin Receptor LYK5 to Regulate Plant Innate Immunity.
Identifieur interne : 000241 ( Main/Exploration ); précédent : 000240; suivant : 000242Arabidopsis CPK5 Phosphorylates the Chitin Receptor LYK5 to Regulate Plant Innate Immunity.
Auteurs : Congcong Huang [République populaire de Chine] ; Yijia Yan [République populaire de Chine] ; Huilin Zhao [République populaire de Chine] ; Ying Ye [République populaire de Chine] ; Yangrong Cao [République populaire de Chine]Source :
- Frontiers in plant science [ 1664-462X ] ; 2020.
Abstract
Chitin, a major component of the fungal cell wall, triggers plant innate immunity in Arabidopsis via a receptor complex including two major lysin motif receptor-like kinases, AtLYK5, and AtCERK1. Although AtLYK5 has been proposed to be a major chitin-binding receptor, the pseudokinase domain of AtLYK5 is required to mediate chitin-triggered immune responses in plants. In this study, 48 AtLYK5-interacting proteins were identified using immunoprecipitation and mass spectrometry assay. Among them, Arabidopsis CALCIUM-DEPENDENT PROTEIN KINASE 5 (AtCPK5) is a protein kinase interacting with both AtLYK5 and AtCERK1. Chitin-induced immune responses are inhibited in both Arabidopsis atcpk5 and atcpk5/6 mutant plants. AtLYK5 and AtLYK4 but not AtCERK1 are phosphorylated by AtCPK5 and AtCPK6 in vitro. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis and in vitro kinase assay identified that Ser-323 and Ser-542 of AtLYK5 are important phosphorylation residues by AtCPK5. Transgenic Arabidopsis expressing either AtLYK5-S323A or AtLYK5-S542A in the atlyk5-2 mutant only partially rescue the defects in chitin-triggered MPK3/MPK6 phosphorylation. Overexpression of AtCPK5 could increase AtCERK1 protein level after chitin treatment. These data proposed a model in which AtCPK5 directly phosphorylates AtLYK5 and regulates chitin-induced defense responses in Arabidopsis.
DOI: 10.3389/fpls.2020.00702
PubMed: 32595659
PubMed Central: PMC7300259
Affiliations:
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type="région">Hubei</region></placeName></affiliation></author><author><name sortKey="Yan, Yijia" sort="Yan, Yijia" uniqKey="Yan Y" first="Yijia" last="Yan">Yijia Yan</name><affiliation wicri:level="3"><nlm:affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan</wicri:regionArea><placeName><settlement type="city">Wuhan</settlement><region type="région">Hubei</region></placeName></affiliation></author><author><name sortKey="Zhao, Huilin" sort="Zhao, Huilin" uniqKey="Zhao H" first="Huilin" last="Zhao">Huilin Zhao</name><affiliation wicri:level="3"><nlm:affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan</wicri:regionArea><placeName><settlement type="city">Wuhan</settlement><region type="région">Hubei</region></placeName></affiliation></author><author><name sortKey="Ye, Ying" sort="Ye, Ying" uniqKey="Ye Y" first="Ying" last="Ye">Ying Ye</name><affiliation wicri:level="3"><nlm:affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan</wicri:regionArea><placeName><settlement 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type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Chitin, a major component of the fungal cell wall, triggers plant innate immunity in <i>Arabidopsis via</i> a receptor complex including two major lysin motif receptor-like kinases, AtLYK5, and AtCERK1. Although AtLYK5 has been proposed to be a major chitin-binding receptor, the pseudokinase domain of AtLYK5 is required to mediate chitin-triggered immune responses in plants. In this study, 48 AtLYK5-interacting proteins were identified using immunoprecipitation and mass spectrometry assay. Among them, <i>Arabidopsis</i> CALCIUM-DEPENDENT PROTEIN KINASE 5 (AtCPK5) is a protein kinase interacting with both AtLYK5 and AtCERK1. Chitin-induced immune responses are inhibited in both <i>Arabidopsis atcpk5</i> and <i>atcpk5/6</i> mutant plants. AtLYK5 and AtLYK4 but not AtCERK1 are phosphorylated by AtCPK5 and AtCPK6 <i>in vitro</i>. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis and <i>in vitro</i> kinase assay identified that Ser-323 and Ser-542 of AtLYK5 are important phosphorylation residues by AtCPK5. Transgenic <i>Arabidopsis</i> expressing either AtLYK5-S323A or AtLYK5-S542A in the <i>atlyk5-2</i> mutant only partially rescue the defects in chitin-triggered MPK3/MPK6 phosphorylation. Overexpression of AtCPK5 could increase AtCERK1 protein level after chitin treatment. These data proposed a model in which AtCPK5 directly phosphorylates AtLYK5 and regulates chitin-induced defense responses in <i>Arabidopsis</i>.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">32595659</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>28</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">1664-462X</ISSN><JournalIssue CitedMedium="Print"><Volume>11</Volume><PubDate><Year>2020</Year></PubDate></JournalIssue><Title>Frontiers in plant science</Title><ISOAbbreviation>Front Plant Sci</ISOAbbreviation></Journal><ArticleTitle><i>Arabidopsis</i> CPK5 Phosphorylates the Chitin Receptor LYK5 to Regulate Plant Innate Immunity.</ArticleTitle><Pagination><MedlinePgn>702</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fpls.2020.00702</ELocationID><Abstract><AbstractText>Chitin, a major component of the fungal cell wall, triggers plant innate immunity in <i>Arabidopsis via</i> a receptor complex including two major lysin motif receptor-like kinases, AtLYK5, and AtCERK1. Although AtLYK5 has been proposed to be a major chitin-binding receptor, the pseudokinase domain of AtLYK5 is required to mediate chitin-triggered immune responses in plants. In this study, 48 AtLYK5-interacting proteins were identified using immunoprecipitation and mass spectrometry assay. Among them, <i>Arabidopsis</i> CALCIUM-DEPENDENT PROTEIN KINASE 5 (AtCPK5) is a protein kinase interacting with both AtLYK5 and AtCERK1. Chitin-induced immune responses are inhibited in both <i>Arabidopsis atcpk5</i> and <i>atcpk5/6</i> mutant plants. AtLYK5 and AtLYK4 but not AtCERK1 are phosphorylated by AtCPK5 and AtCPK6 <i>in vitro</i>. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis and <i>in vitro</i> kinase assay identified that Ser-323 and Ser-542 of AtLYK5 are important phosphorylation residues by AtCPK5. Transgenic <i>Arabidopsis</i> expressing either AtLYK5-S323A or AtLYK5-S542A in the <i>atlyk5-2</i> mutant only partially rescue the defects in chitin-triggered MPK3/MPK6 phosphorylation. Overexpression of AtCPK5 could increase AtCERK1 protein level after chitin treatment. These data proposed a model in which AtCPK5 directly phosphorylates AtLYK5 and regulates chitin-induced defense responses in <i>Arabidopsis</i>.</AbstractText><CopyrightInformation>Copyright © 2020 Huang, Yan, Zhao, Ye and Cao.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Congcong</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yan</LastName><ForeName>Yijia</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan, China.</Affiliation></AffiliationInfo></Author><Author 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