A bacterial effector protein prevents MAPK-mediated phosphorylation of SGT1 to suppress plant immunity.
Identifieur interne : 000234 ( Main/Exploration ); précédent : 000233; suivant : 000235A bacterial effector protein prevents MAPK-mediated phosphorylation of SGT1 to suppress plant immunity.
Auteurs : Gang Yu [République populaire de Chine] ; Liu Xian [République populaire de Chine] ; Hao Xue [République populaire de Chine] ; Wenjia Yu [République populaire de Chine] ; Jose S. Rufian [République populaire de Chine] ; Yuying Sang [République populaire de Chine] ; Rafael J L. Morcillo [République populaire de Chine] ; Yaru Wang [République populaire de Chine] ; Alberto P. Macho [République populaire de Chine]Source :
- PLoS pathogens [ 1553-7374 ] ; 2020.
Descripteurs français
- KwdFr :
- Immunité des plantes (immunologie), Maladies des plantes (immunologie), Mitogen-Activated Protein Kinases (métabolisme), Phosphorylation (MeSH), Protéines bactériennes (métabolisme), Protéines végétales (immunologie), Protéines végétales (métabolisme), Ralstonia solanacearum (immunologie), Ralstonia solanacearum (métabolisme), Tabac (métabolisme).
- MESH :
English descriptors
- KwdEn :
- Bacterial Proteins (metabolism), Mitogen-Activated Protein Kinases (metabolism), Phosphorylation (MeSH), Plant Diseases (immunology), Plant Immunity (immunology), Plant Proteins (immunology), Plant Proteins (metabolism), Ralstonia solanacearum (immunology), Ralstonia solanacearum (metabolism), Tobacco (metabolism).
- MESH :
- chemical , immunology : Plant Proteins.
- chemical , metabolism : Bacterial Proteins, Mitogen-Activated Protein Kinases, Plant Proteins.
- immunology : Plant Diseases, Plant Immunity, Ralstonia solanacearum.
- metabolism : Ralstonia solanacearum, Tobacco.
- Phosphorylation.
Abstract
Nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins function as sensors that perceive pathogen molecules and activate immunity. In plants, the accumulation and activation of NLRs is regulated by SUPPRESSOR OF G2 ALLELE OF skp1 (SGT1). In this work, we found that an effector protein named RipAC, secreted by the plant pathogen Ralstonia solanacearum, associates with SGT1 to suppress NLR-mediated SGT1-dependent immune responses, including those triggered by another R. solanacearum effector, RipE1. RipAC does not affect the accumulation of SGT1 or NLRs, or their interaction. However, RipAC inhibits the interaction between SGT1 and MAP kinases, and the phosphorylation of a MAPK target motif in the C-terminal domain of SGT1. Such phosphorylation is enhanced upon activation of immune signaling and contributes to the activation of immune responses mediated by the NLR RPS2. Additionally, SGT1 phosphorylation contributes to resistance against R. solanacearum. Our results shed light onto the mechanism of activation of NLR-mediated immunity, and suggest a positive feedback loop between MAPK activation and SGT1-dependent NLR activation.
DOI: 10.1371/journal.ppat.1008933
PubMed: 32976518
PubMed Central: PMC7540872
Affiliations:
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Le document en format XML
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Rufian</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation></author><author><name sortKey="Sang, Yuying" sort="Sang, Yuying" uniqKey="Sang Y" first="Yuying" last="Sang">Yuying Sang</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation></author><author><name sortKey="Morcillo, Rafael J L" sort="Morcillo, Rafael J L" uniqKey="Morcillo R" first="Rafael J L" last="Morcillo">Rafael J L. Morcillo</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation></author><author><name sortKey="Wang, Yaru" sort="Wang, Yaru" uniqKey="Wang Y" first="Yaru" last="Wang">Yaru Wang</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation><affiliation wicri:level="3"><nlm:affiliation>University of Chinese Academy of Sciences, Beijing, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>University of Chinese Academy of Sciences, Beijing</wicri:regionArea><placeName><settlement type="city">Pékin</settlement></placeName></affiliation></author><author><name sortKey="Macho, Alberto P" sort="Macho, Alberto P" uniqKey="Macho A" first="Alberto P" last="Macho">Alberto P. Macho</name><affiliation wicri:level="1"><nlm:affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai</wicri:regionArea><wicri:noRegion>Shanghai</wicri:noRegion></affiliation></author></analytic><series><title level="j">PLoS pathogens</title><idno type="eISSN">1553-7374</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (metabolism)</term><term>Mitogen-Activated Protein Kinases (metabolism)</term><term>Phosphorylation (MeSH)</term><term>Plant Diseases (immunology)</term><term>Plant Immunity (immunology)</term><term>Plant Proteins (immunology)</term><term>Plant Proteins (metabolism)</term><term>Ralstonia solanacearum (immunology)</term><term>Ralstonia solanacearum (metabolism)</term><term>Tobacco (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Immunité des plantes (immunologie)</term><term>Maladies des plantes (immunologie)</term><term>Mitogen-Activated Protein Kinases (métabolisme)</term><term>Phosphorylation (MeSH)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines végétales (immunologie)</term><term>Protéines végétales (métabolisme)</term><term>Ralstonia solanacearum (immunologie)</term><term>Ralstonia solanacearum (métabolisme)</term><term>Tabac (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>Plant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Mitogen-Activated Protein Kinases</term><term>Plant Proteins</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Immunité des plantes</term><term>Maladies des plantes</term><term>Protéines végétales</term><term>Ralstonia solanacearum</term></keywords><keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Plant Diseases</term><term>Plant Immunity</term><term>Ralstonia solanacearum</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Ralstonia solanacearum</term><term>Tobacco</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Mitogen-Activated Protein Kinases</term><term>Protéines bactériennes</term><term>Protéines végétales</term><term>Ralstonia solanacearum</term><term>Tabac</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Phosphorylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins function as sensors that perceive pathogen molecules and activate immunity. In plants, the accumulation and activation of NLRs is regulated by SUPPRESSOR OF G2 ALLELE OF skp1 (SGT1). In this work, we found that an effector protein named RipAC, secreted by the plant pathogen Ralstonia solanacearum, associates with SGT1 to suppress NLR-mediated SGT1-dependent immune responses, including those triggered by another R. solanacearum effector, RipE1. RipAC does not affect the accumulation of SGT1 or NLRs, or their interaction. However, RipAC inhibits the interaction between SGT1 and MAP kinases, and the phosphorylation of a MAPK target motif in the C-terminal domain of SGT1. Such phosphorylation is enhanced upon activation of immune signaling and contributes to the activation of immune responses mediated by the NLR RPS2. Additionally, SGT1 phosphorylation contributes to resistance against R. solanacearum. Our results shed light onto the mechanism of activation of NLR-mediated immunity, and suggest a positive feedback loop between MAPK activation and SGT1-dependent NLR activation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32976518</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>12</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>12</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1553-7374</ISSN><JournalIssue CitedMedium="Internet"><Volume>16</Volume><Issue>9</Issue><PubDate><Year>2020</Year><Month>09</Month></PubDate></JournalIssue><Title>PLoS pathogens</Title><ISOAbbreviation>PLoS Pathog</ISOAbbreviation></Journal><ArticleTitle>A bacterial effector protein prevents MAPK-mediated phosphorylation of SGT1 to suppress plant immunity.</ArticleTitle><Pagination><MedlinePgn>e1008933</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.ppat.1008933</ELocationID><Abstract><AbstractText>Nucleotide-binding domain and leucine-rich repeat-containing (NLR) proteins function as sensors that perceive pathogen molecules and activate immunity. In plants, the accumulation and activation of NLRs is regulated by SUPPRESSOR OF G2 ALLELE OF skp1 (SGT1). In this work, we found that an effector protein named RipAC, secreted by the plant pathogen Ralstonia solanacearum, associates with SGT1 to suppress NLR-mediated SGT1-dependent immune responses, including those triggered by another R. solanacearum effector, RipE1. RipAC does not affect the accumulation of SGT1 or NLRs, or their interaction. However, RipAC inhibits the interaction between SGT1 and MAP kinases, and the phosphorylation of a MAPK target motif in the C-terminal domain of SGT1. Such phosphorylation is enhanced upon activation of immune signaling and contributes to the activation of immune responses mediated by the NLR RPS2. Additionally, SGT1 phosphorylation contributes to resistance against R. solanacearum. Our results shed light onto the mechanism of activation of NLR-mediated immunity, and suggest a positive feedback loop between MAPK activation and SGT1-dependent NLR activation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Gang</ForeName><Initials>G</Initials><Identifier Source="ORCID">0000-0002-6720-7490</Identifier><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xian</LastName><ForeName>Liu</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>University of Chinese Academy of Sciences, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Xue</LastName><ForeName>Hao</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>University of Chinese Academy of Sciences, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yu</LastName><ForeName>Wenjia</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>University of Chinese Academy of Sciences, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rufian</LastName><ForeName>Jose S</ForeName><Initials>JS</Initials><Identifier Source="ORCID">0000-0002-3871-3706</Identifier><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sang</LastName><ForeName>Yuying</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morcillo</LastName><ForeName>Rafael J L</ForeName><Initials>RJL</Initials><Identifier Source="ORCID">0000-0002-0546-5195</Identifier><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yaru</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>University of Chinese Academy of Sciences, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Macho</LastName><ForeName>Alberto P</ForeName><Initials>AP</Initials><Identifier Source="ORCID">0000-0001-9935-8026</Identifier><AffiliationInfo><Affiliation>Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of Sciences, Shanghai, China.</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>09</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS Pathog</MedlineTA><NlmUniqueID>101238921</NlmUniqueID><ISSNLinking>1553-7366</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.24</RegistryNumber><NameOfSubstance UI="D020928">Mitogen-Activated Protein Kinases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000378" 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