Arabidopsis Lectin Receptor Kinase P2K2 Is a Second Plant Receptor for Extracellular ATP and Contributes to Innate Immunity.
Identifieur interne : 000209 ( Main/Exploration ); précédent : 000208; suivant : 000210Arabidopsis Lectin Receptor Kinase P2K2 Is a Second Plant Receptor for Extracellular ATP and Contributes to Innate Immunity.
Auteurs : An Quoc Pham [États-Unis] ; Sung-Hwan Cho [États-Unis] ; Cuong The Nguyen [États-Unis, Viêt Nam] ; Gary Stacey [États-Unis]Source :
- Plant physiology [ 1532-2548 ] ; 2020.
Abstract
In animals, extracellular ATP is a well-studied signaling molecule that is recognized by plasma membrane-localized P2-type purinergic receptors. However, in contrast, much less is known about purinergic signaling in plants. P2 receptors play critical roles in a variety of animal biological processes, including immune system regulation. The first plant purinergic receptor, Arabidopsis (Arabidopsis thaliana) P2K1 (L-type lectin receptor kinase-I.9), was shown to contribute to plant defense against bacterial, oomycete, and fungal pathogens. Here, we demonstrate the isolation of a second purinergic receptor, P2K2, by complementation of an Arabidopsis p2k1 mutant. P2K2 (LecRK-I.5) has 74% amino acid similarity to P2K1. The P2K2 extracellular lectin domain binds to ATP with higher affinity than P2K1 (dissociation constant [Kd] = 44.47 ± 15.73 nm). Interestingly, p2k2 and p2k1 p2k2 mutant plants showed increased susceptibility to the pathogen Pseudomonas syringae, with the double mutant showing a stronger phenotype. In vitro and in planta studies demonstrate that P2K2 and P2K1 interact and cross-phosphorylate upon extracellular ATP treatment. Thus, similar to animals, plants possess multiple purinergic receptors.
DOI: 10.1104/pp.19.01265
PubMed: 32345768
PubMed Central: PMC7333714
Affiliations:
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Bond Life Science Center, University of Missouri, Columbia</wicri:cityArea></affiliation></author><author><name sortKey="Nguyen, Cuong The" sort="Nguyen, Cuong The" uniqKey="Nguyen C" first="Cuong The" last="Nguyen">Cuong The Nguyen</name><affiliation wicri:level="2"><nlm:affiliation>Divisions of Plant Science and Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, Missouri 65211.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Missouri (État)</region></placeName><wicri:cityArea>Divisions of Plant Science and Biochemistry, C.S. 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Bond Life Science Center, University of Missouri, Columbia</wicri:regionArea><wicri:noRegion>Columbia</wicri:noRegion></affiliation></author></analytic><series><title level="j">Plant physiology</title><idno type="eISSN">1532-2548</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In animals, extracellular ATP is a well-studied signaling molecule that is recognized by plasma membrane-localized P2-type purinergic receptors. However, in contrast, much less is known about purinergic signaling in plants. P2 receptors play critical roles in a variety of animal biological processes, including immune system regulation. The first plant purinergic receptor, Arabidopsis (<i>Arabidopsis thaliana</i>) P2K1 (L-type lectin receptor kinase-I.9), was shown to contribute to plant defense against bacterial, oomycete, and fungal pathogens. Here, we demonstrate the isolation of a second purinergic receptor, P2K2, by complementation of an Arabidopsis <i>p2k1</i> mutant. P2K2 (LecRK-I.5) has 74% amino acid similarity to P2K1. The P2K2 extracellular lectin domain binds to ATP with higher affinity than P2K1 (dissociation constant [<i>K</i><sub>d</sub>] = 44.47 ± 15.73 nm). Interestingly, <i>p2k2</i> and <i>p2k1 p2k2</i> mutant plants showed increased susceptibility to the pathogen <i>Pseudomonas syringae,</i> with the double mutant showing a stronger phenotype. In vitro and in planta studies demonstrate that P2K2 and P2K1 interact and cross-phosphorylate upon extracellular ATP treatment. Thus, similar to animals, plants possess multiple purinergic receptors.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32345768</PMID><DateRevised><Year>2020</Year><Month>08</Month><Day>03</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1532-2548</ISSN><JournalIssue CitedMedium="Internet"><Volume>183</Volume><Issue>3</Issue><PubDate><Year>2020</Year><Month>07</Month></PubDate></JournalIssue><Title>Plant physiology</Title><ISOAbbreviation>Plant Physiol</ISOAbbreviation></Journal><ArticleTitle>Arabidopsis Lectin Receptor Kinase P2K2 Is a Second Plant Receptor for Extracellular ATP and Contributes to Innate Immunity.</ArticleTitle><Pagination><MedlinePgn>1364-1375</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1104/pp.19.01265</ELocationID><Abstract><AbstractText>In animals, extracellular ATP is a well-studied signaling molecule that is recognized by plasma membrane-localized P2-type purinergic receptors. However, in contrast, much less is known about purinergic signaling in plants. P2 receptors play critical roles in a variety of animal biological processes, including immune system regulation. The first plant purinergic receptor, Arabidopsis (<i>Arabidopsis thaliana</i>) P2K1 (L-type lectin receptor kinase-I.9), was shown to contribute to plant defense against bacterial, oomycete, and fungal pathogens. Here, we demonstrate the isolation of a second purinergic receptor, P2K2, by complementation of an Arabidopsis <i>p2k1</i> mutant. P2K2 (LecRK-I.5) has 74% amino acid similarity to P2K1. The P2K2 extracellular lectin domain binds to ATP with higher affinity than P2K1 (dissociation constant [<i>K</i><sub>d</sub>] = 44.47 ± 15.73 nm). Interestingly, <i>p2k2</i> and <i>p2k1 p2k2</i> mutant plants showed increased susceptibility to the pathogen <i>Pseudomonas syringae,</i> with the double mutant showing a stronger phenotype. In vitro and in planta studies demonstrate that P2K2 and P2K1 interact and cross-phosphorylate upon extracellular ATP treatment. Thus, similar to animals, plants possess multiple purinergic receptors.</AbstractText><CopyrightInformation>© 2020 American Society of Plant Biologists. All Rights Reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pham</LastName><ForeName>An Quoc</ForeName><Initials>AQ</Initials><Identifier Source="ORCID">0000-0001-8904-9975</Identifier><AffiliationInfo><Affiliation>Divisions of Plant Science and Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, Missouri 65211.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Cho</LastName><ForeName>Sung-Hwan</ForeName><Initials>SH</Initials><Identifier Source="ORCID">0000-0003-2230-2037</Identifier><AffiliationInfo><Affiliation>Divisions of Plant Science and Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, Missouri 65211.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nguyen</LastName><ForeName>Cuong The</ForeName><Initials>CT</Initials><AffiliationInfo><Affiliation>Divisions of Plant Science and Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, Missouri 65211.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Cuu Long Delta Rice Research Institute, Cantho 00000, Vietnam.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stacey</LastName><ForeName>Gary</ForeName><Initials>G</Initials><Identifier Source="ORCID">0000-0001-5914-2247</Identifier><AffiliationInfo><Affiliation>Divisions of Plant Science and Biochemistry, C.S. Bond Life Science Center, University of Missouri, Columbia, Missouri 65211 staceyg@missouri.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 GM121445</GrantID><Acronym>GM</Acronym><Agency>NIGMS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>04</Month><Day>28</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Plant 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