The rice LysM receptor-like kinase OsCERK1 is required for the perception of short-chain chitin oligomers in arbuscular mycorrhizal signaling.
Identifieur interne : 000D22 ( Main/Corpus ); précédent : 000D21; suivant : 000D23The rice LysM receptor-like kinase OsCERK1 is required for the perception of short-chain chitin oligomers in arbuscular mycorrhizal signaling.
Auteurs : Gennaro Carotenuto ; Mireille Chabaud ; Kana Miyata ; Martina Capozzi ; Naoya Takeda ; Hanae Kaku ; Naoto Shibuya ; Tomomi Nakagawa ; David G. Barker ; Andrea GenreSource :
- The New phytologist [ 1469-8137 ] ; 2017.
English descriptors
- KwdEn :
- Calcium (metabolism), Chitin (metabolism), Gene Knockout Techniques (MeSH), Mutation (MeSH), Mycorrhizae (metabolism), Mycorrhizae (physiology), Oryza (genetics), Oryza (metabolism), Oryza (microbiology), Plant Proteins (genetics), Plant Proteins (metabolism), Plant Roots (metabolism), Plant Roots (microbiology), Protein-Serine-Threonine Kinases (genetics), Protein-Serine-Threonine Kinases (metabolism), Signal Transduction (MeSH).
- MESH :
- chemical , genetics : Plant Proteins, Protein-Serine-Threonine Kinases.
- chemical , metabolism : Calcium, Chitin, Plant Proteins, Protein-Serine-Threonine Kinases.
- genetics : Oryza.
- metabolism : Mycorrhizae, Oryza, Plant Roots.
- microbiology : Oryza, Plant Roots.
- physiology : Mycorrhizae.
- Gene Knockout Techniques, Mutation, Signal Transduction.
Abstract
The rice lysin-motif (LysM) receptor-like kinase OsCERK1 is now known to have a dual role in both pathogenic and symbiotic interactions. Following the recent discovery that the Oscerk1 mutant is unable to host arbuscular mycorrhizal (AM) fungi, we have examined whether OsCERK1 is directly involved in the perception of the short-chain chitin oligomers (Myc-COs) identified in AM fungal exudates and shown to activate nuclear calcium (Ca2+ ) spiking in the rice root epidermis. An Oscerk1 knockout mutant expressing the cameleon NLS-YC2.60 was used to monitor nuclear Ca2+ signaling following root treatment with either crude fungal exudates or purified Myc-COs. Compared with wild-type rice, Ca2+ spiking responses to AM fungal elicitation were absent in root atrichoblasts of the Oscerk1 mutant. By contrast, rice lines mutated in OsCEBiP, encoding the LysM receptor-like protein which associates with OsCERK1 to perceive chitin elicitors of the host immune defense pathway, responded positively to Myc-COs. These findings provide direct evidence that the bi-functional OsCERK1 plays a central role in perceiving short-chain Myc-CO signals and activating the downstream conserved symbiotic signal transduction pathway.
DOI: 10.1111/nph.14539
PubMed: 28369864
Links to Exploration step
pubmed:28369864Le document en format XML
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Barker</name><affiliation><nlm:affiliation>Laboratory of Plant-Microbe Interactions (LIPM), INRA-CNRS-Toulouse University, Castanet-Tolosan, 31326, France.</nlm:affiliation></affiliation></author><author><name sortKey="Genre, Andrea" sort="Genre, Andrea" uniqKey="Genre A" first="Andrea" last="Genre">Andrea Genre</name><affiliation><nlm:affiliation>Department of Life Sciences and Systems Biology, University of Torino, Torino, 10125, Italy.</nlm:affiliation></affiliation></author></analytic><series><title level="j">The New phytologist</title><idno type="eISSN">1469-8137</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Calcium (metabolism)</term><term>Chitin (metabolism)</term><term>Gene Knockout Techniques (MeSH)</term><term>Mutation (MeSH)</term><term>Mycorrhizae (metabolism)</term><term>Mycorrhizae (physiology)</term><term>Oryza (genetics)</term><term>Oryza (metabolism)</term><term>Oryza (microbiology)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (metabolism)</term><term>Plant Roots (metabolism)</term><term>Plant Roots (microbiology)</term><term>Protein-Serine-Threonine Kinases (genetics)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Signal Transduction (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term><term>Chitin</term><term>Plant Proteins</term><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Oryza</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Mycorrhizae</term><term>Oryza</term><term>Plant Roots</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Oryza</term><term>Plant Roots</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mycorrhizae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Gene Knockout Techniques</term><term>Mutation</term><term>Signal Transduction</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The rice lysin-motif (LysM) receptor-like kinase OsCERK1 is now known to have a dual role in both pathogenic and symbiotic interactions. Following the recent discovery that the Oscerk1 mutant is unable to host arbuscular mycorrhizal (AM) fungi, we have examined whether OsCERK1 is directly involved in the perception of the short-chain chitin oligomers (Myc-COs) identified in AM fungal exudates and shown to activate nuclear calcium (Ca<sup>2+</sup> ) spiking in the rice root epidermis. An Oscerk1 knockout mutant expressing the cameleon NLS-YC2.60 was used to monitor nuclear Ca<sup>2+</sup> signaling following root treatment with either crude fungal exudates or purified Myc-COs. Compared with wild-type rice, Ca<sup>2+</sup> spiking responses to AM fungal elicitation were absent in root atrichoblasts of the Oscerk1 mutant. By contrast, rice lines mutated in OsCEBiP, encoding the LysM receptor-like protein which associates with OsCERK1 to perceive chitin elicitors of the host immune defense pathway, responded positively to Myc-COs. These findings provide direct evidence that the bi-functional OsCERK1 plays a central role in perceiving short-chain Myc-CO signals and activating the downstream conserved symbiotic signal transduction pathway.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28369864</PMID><DateCompleted><Year>2018</Year><Month>02</Month><Day>22</Day></DateCompleted><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1469-8137</ISSN><JournalIssue CitedMedium="Internet"><Volume>214</Volume><Issue>4</Issue><PubDate><Year>2017</Year><Month>Jun</Month></PubDate></JournalIssue><Title>The New phytologist</Title><ISOAbbreviation>New Phytol</ISOAbbreviation></Journal><ArticleTitle>The rice LysM receptor-like kinase OsCERK1 is required for the perception of short-chain chitin oligomers in arbuscular mycorrhizal signaling.</ArticleTitle><Pagination><MedlinePgn>1440-1446</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1111/nph.14539</ELocationID><Abstract><AbstractText>The rice lysin-motif (LysM) receptor-like kinase OsCERK1 is now known to have a dual role in both pathogenic and symbiotic interactions. Following the recent discovery that the Oscerk1 mutant is unable to host arbuscular mycorrhizal (AM) fungi, we have examined whether OsCERK1 is directly involved in the perception of the short-chain chitin oligomers (Myc-COs) identified in AM fungal exudates and shown to activate nuclear calcium (Ca<sup>2+</sup> ) spiking in the rice root epidermis. An Oscerk1 knockout mutant expressing the cameleon NLS-YC2.60 was used to monitor nuclear Ca<sup>2+</sup> signaling following root treatment with either crude fungal exudates or purified Myc-COs. Compared with wild-type rice, Ca<sup>2+</sup> spiking responses to AM fungal elicitation were absent in root atrichoblasts of the Oscerk1 mutant. By contrast, rice lines mutated in OsCEBiP, encoding the LysM receptor-like protein which associates with OsCERK1 to perceive chitin elicitors of the host immune defense pathway, responded positively to Myc-COs. These findings provide direct evidence that the bi-functional OsCERK1 plays a central role in perceiving short-chain Myc-CO signals and activating the downstream conserved symbiotic signal transduction pathway.</AbstractText><CopyrightInformation>© 2017 The Authors. New Phytologist © 2017 New Phytologist Trust.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Carotenuto</LastName><ForeName>Gennaro</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Life Sciences and Systems Biology, University of Torino, Torino, 10125, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chabaud</LastName><ForeName>Mireille</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Plant-Microbe Interactions (LIPM), INRA-CNRS-Toulouse University, Castanet-Tolosan, 31326, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Miyata</LastName><ForeName>Kana</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, School of Agriculture, Meiji University, Kawasaki, Kanagawa, 214-8571, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Capozzi</LastName><ForeName>Martina</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Life Sciences and Systems Biology, University of Torino, Torino, 10125, Italy.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Takeda</LastName><ForeName>Naoya</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>National Institute for Basic Biology (NIBB)/SOKENDAI, Nishigonaka 38, Myodaiji, Okazaki, Aichi, 444-8585, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kaku</LastName><ForeName>Hanae</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, School of Agriculture, Meiji University, Kawasaki, Kanagawa, 214-8571, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Shibuya</LastName><ForeName>Naoto</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Life Sciences, School of Agriculture, Meiji University, Kawasaki, Kanagawa, 214-8571, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nakagawa</LastName><ForeName>Tomomi</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>National Institute for Basic Biology (NIBB)/SOKENDAI, Nishigonaka 38, Myodaiji, Okazaki, Aichi, 444-8585, Japan.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Division of Biological Science, Graduate School of Science, Nagoya University, Nagoya, Aichi, 464-8602, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Barker</LastName><ForeName>David G</ForeName><Initials>DG</Initials><AffiliationInfo><Affiliation>Laboratory of Plant-Microbe Interactions (LIPM), INRA-CNRS-Toulouse University, Castanet-Tolosan, 31326, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Genre</LastName><ForeName>Andrea</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Life Sciences and Systems Biology, University of Torino, Torino, 10125, Italy.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>03</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>New Phytol</MedlineTA><NlmUniqueID>9882884</NlmUniqueID><ISSNLinking>0028-646X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>1398-61-4</RegistryNumber><NameOfSubstance UI="D002686">Chitin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber><NameOfSubstance UI="D002118">Calcium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002686" MajorTopicYN="N">Chitin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D055786" MajorTopicYN="N">Gene Knockout Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009154" MajorTopicYN="N">Mutation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D038821" MajorTopicYN="N">Mycorrhizae</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012275" MajorTopicYN="N">Oryza</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="Y">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018517" MajorTopicYN="N">Plant Roots</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000382" MajorTopicYN="N">microbiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017346" MajorTopicYN="N">Protein-Serine-Threonine Kinases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Oryza sativa
</Keyword><Keyword MajorTopicYN="N">LysM receptor-like kinase (RLK)</Keyword><Keyword MajorTopicYN="N">arbuscular mycorrhiza (AM)</Keyword><Keyword MajorTopicYN="N">chitin oligomer signaling</Keyword><Keyword MajorTopicYN="N">nuclear calcium spiking</Keyword><Keyword MajorTopicYN="N">plant-microbe interactions</Keyword><Keyword MajorTopicYN="N">root symbiosis</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year><Month>10</Month><Day>11</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>02</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>2</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>4</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28369864</ArticleId><ArticleId IdType="doi">10.1111/nph.14539</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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