Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms.
Identifieur interne : 000085 ( Main/Exploration ); précédent : 000084; suivant : 000086Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms.
Auteurs : Hailong Guo [Royaume-Uni] ; Hee-Kyung Ahn [Royaume-Uni] ; Jan Sklenar [Royaume-Uni] ; Jianhua Huang [Royaume-Uni] ; Yan Ma [Royaume-Uni] ; Pingtao Ding [Royaume-Uni] ; Frank L H. Menke [Royaume-Uni] ; Jonathan D G. Jones [Royaume-Uni]Source :
- Cell host & microbe [ 1934-6069 ] ; 2020.
Abstract
The Arabidopsis immune receptors RPS4 and RRS1 interact to co-confer responsiveness to bacterial effectors. The RRS1-R allele, with RPS4, responds to AvrRps4 and PopP2, whereas RRS1-S responds only to AvrRps4. Here, we show that the C terminus of RRS1-R but not RRS1-S is phosphorylated. Phosphorylation at Thr1214 in the WRKY domain maintains RRS1-R in its inactive state and also inhibits acetylation of RRS1-R by PopP2. PopP2 in turn catalyzes O-acetylation at the same site, thereby preventing its phosphorylation. Phosphorylation at other sites is required for PopP2 but not AvrRps4 responsiveness and facilitates the interaction of RRS1's C terminus with its TIR domain. Derepression of RRS1-R or RRS1-S involves effector-triggered proximity between their TIR domain and C termini. This effector-promoted interaction between these domains relieves inhibition of TIRRPS4 by TIRRRS1. Our data reveal effector-triggered and phosphorylation-regulated conformational changes within RRS1 that results in distinct modes of derepression of the complex by PopP2 and AvrRps4.
DOI: 10.1016/j.chom.2020.03.008
PubMed: 32234500
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Electronic address: jonathan.jones@tsl.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2020">2020</date><idno type="RBID">pubmed:32234500</idno><idno type="pmid">32234500</idno><idno type="doi">10.1016/j.chom.2020.03.008</idno><idno type="wicri:Area/Main/Corpus">000178</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000178</idno><idno type="wicri:Area/Main/Curation">000178</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000178</idno><idno type="wicri:Area/Main/Exploration">000178</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms.</title><author><name sortKey="Guo, Hailong" sort="Guo, Hailong" uniqKey="Guo H" first="Hailong" last="Guo">Hailong Guo</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Ahn, Hee Kyung" sort="Ahn, Hee Kyung" uniqKey="Ahn H" first="Hee-Kyung" last="Ahn">Hee-Kyung Ahn</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Sklenar, Jan" sort="Sklenar, Jan" uniqKey="Sklenar J" first="Jan" last="Sklenar">Jan Sklenar</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Huang, Jianhua" sort="Huang, Jianhua" uniqKey="Huang J" first="Jianhua" last="Huang">Jianhua Huang</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Ding, Pingtao" sort="Ding, Pingtao" uniqKey="Ding P" first="Pingtao" last="Ding">Pingtao Ding</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Menke, Frank L H" sort="Menke, Frank L H" uniqKey="Menke F" first="Frank L H" last="Menke">Frank L H. Menke</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author><author><name sortKey="Jones, Jonathan D G" sort="Jones, Jonathan D G" uniqKey="Jones J" first="Jonathan D G" last="Jones">Jonathan D G. Jones</name><affiliation wicri:level="1"><nlm:affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK. Electronic address: jonathan.jones@tsl.ac.uk.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH</wicri:regionArea><wicri:noRegion>Norwich NR4 7UH</wicri:noRegion></affiliation></author></analytic><series><title level="j">Cell host & microbe</title><idno type="eISSN">1934-6069</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">The Arabidopsis immune receptors RPS4 and RRS1 interact to co-confer responsiveness to bacterial effectors. The RRS1-R allele, with RPS4, responds to AvrRps4 and PopP2, whereas RRS1-S responds only to AvrRps4. Here, we show that the C terminus of RRS1-R but not RRS1-S is phosphorylated. Phosphorylation at Thr1214 in the WRKY domain maintains RRS1-R in its inactive state and also inhibits acetylation of RRS1-R by PopP2. PopP2 in turn catalyzes O-acetylation at the same site, thereby preventing its phosphorylation. Phosphorylation at other sites is required for PopP2 but not AvrRps4 responsiveness and facilitates the interaction of RRS1's C terminus with its TIR domain. Derepression of RRS1-R or RRS1-S involves effector-triggered proximity between their TIR domain and C termini. This effector-promoted interaction between these domains relieves inhibition of TIR<sup>RPS4</sup> by TIR<sup>RRS1</sup>. Our data reveal effector-triggered and phosphorylation-regulated conformational changes within RRS1 that results in distinct modes of derepression of the complex by PopP2 and AvrRps4.</div></front></TEI><pubmed><MedlineCitation Status="In-Process" Owner="NLM"><PMID Version="1">32234500</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1934-6069</ISSN><JournalIssue CitedMedium="Internet"><Volume>27</Volume><Issue>5</Issue><PubDate><Year>2020</Year><Month>05</Month><Day>13</Day></PubDate></JournalIssue><Title>Cell host & microbe</Title><ISOAbbreviation>Cell Host Microbe</ISOAbbreviation></Journal><ArticleTitle>Phosphorylation-Regulated Activation of the Arabidopsis RRS1-R/RPS4 Immune Receptor Complex Reveals Two Distinct Effector Recognition Mechanisms.</ArticleTitle><Pagination><MedlinePgn>769-781.e6</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S1931-3128(20)30172-4</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.chom.2020.03.008</ELocationID><Abstract><AbstractText>The Arabidopsis immune receptors RPS4 and RRS1 interact to co-confer responsiveness to bacterial effectors. The RRS1-R allele, with RPS4, responds to AvrRps4 and PopP2, whereas RRS1-S responds only to AvrRps4. Here, we show that the C terminus of RRS1-R but not RRS1-S is phosphorylated. Phosphorylation at Thr1214 in the WRKY domain maintains RRS1-R in its inactive state and also inhibits acetylation of RRS1-R by PopP2. PopP2 in turn catalyzes O-acetylation at the same site, thereby preventing its phosphorylation. Phosphorylation at other sites is required for PopP2 but not AvrRps4 responsiveness and facilitates the interaction of RRS1's C terminus with its TIR domain. Derepression of RRS1-R or RRS1-S involves effector-triggered proximity between their TIR domain and C termini. This effector-promoted interaction between these domains relieves inhibition of TIR<sup>RPS4</sup> by TIR<sup>RRS1</sup>. Our data reveal effector-triggered and phosphorylation-regulated conformational changes within RRS1 that results in distinct modes of derepression of the complex by PopP2 and AvrRps4.</AbstractText><CopyrightInformation>Copyright © 2020. Published by Elsevier Inc.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Hailong</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahn</LastName><ForeName>Hee-Kyung</ForeName><Initials>HK</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sklenar</LastName><ForeName>Jan</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Huang</LastName><ForeName>Jianhua</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ding</LastName><ForeName>Pingtao</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Menke</LastName><ForeName>Frank L H</ForeName><Initials>FLH</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jones</LastName><ForeName>Jonathan D G</ForeName><Initials>JDG</Initials><AffiliationInfo><Affiliation>The Sainsbury Laboratory, University of East Anglia, Norwich Research Park, Norwich NR4 7UH, UK. Electronic address: jonathan.jones@tsl.ac.uk.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>03</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Cell Host Microbe</MedlineTA><NlmUniqueID>101302316</NlmUniqueID><ISSNLinking>1931-3128</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="CommentIn"><RefSource>Trends Plant Sci. 2020 Sep;25(9):836-838</RefSource><PMID Version="1">32595088</PMID></CommentsCorrections></CommentsCorrectionsList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">acetylation</Keyword><Keyword MajorTopicYN="Y">effector-triggered immunity</Keyword><Keyword MajorTopicYN="Y">integrated decoy</Keyword><Keyword MajorTopicYN="Y">paired NLR immune receptors</Keyword><Keyword MajorTopicYN="Y">phosphorylation</Keyword><Keyword MajorTopicYN="Y">plant-disease resistance</Keyword></KeywordList><CoiStatement>Declaration of Interests The authors declare no competing interests.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>08</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2019</Year><Month>12</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>03</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>4</Month><Day>3</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32234500</ArticleId><ArticleId IdType="pii">S1931-3128(20)30172-4</ArticleId><ArticleId IdType="doi">10.1016/j.chom.2020.03.008</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><country name="Royaume-Uni"><noRegion><name sortKey="Guo, Hailong" sort="Guo, Hailong" uniqKey="Guo H" first="Hailong" last="Guo">Hailong Guo</name></noRegion><name sortKey="Ahn, Hee Kyung" sort="Ahn, Hee Kyung" uniqKey="Ahn H" first="Hee-Kyung" last="Ahn">Hee-Kyung Ahn</name><name sortKey="Ding, Pingtao" sort="Ding, Pingtao" uniqKey="Ding P" first="Pingtao" last="Ding">Pingtao Ding</name><name sortKey="Huang, Jianhua" sort="Huang, Jianhua" uniqKey="Huang J" first="Jianhua" last="Huang">Jianhua Huang</name><name sortKey="Jones, Jonathan D G" sort="Jones, Jonathan D G" uniqKey="Jones J" first="Jonathan D G" last="Jones">Jonathan D G. Jones</name><name sortKey="Ma, Yan" sort="Ma, Yan" uniqKey="Ma Y" first="Yan" last="Ma">Yan Ma</name><name sortKey="Menke, Frank L H" sort="Menke, Frank L H" uniqKey="Menke F" first="Frank L H" last="Menke">Frank L H. Menke</name><name sortKey="Sklenar, Jan" sort="Sklenar, Jan" uniqKey="Sklenar J" first="Jan" last="Sklenar">Jan Sklenar</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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