SlRLK-like is a malectin-like domain protein affecting localization and abundance of LeEIX2 receptor resulting in suppression of EIX-induced immune responses.
Identifieur interne : 000051 ( Main/Exploration ); précédent : 000050; suivant : 000052SlRLK-like is a malectin-like domain protein affecting localization and abundance of LeEIX2 receptor resulting in suppression of EIX-induced immune responses.
Auteurs : Orian Sussholz [Israël] ; Lorena Pizarro [Israël] ; Silvia Schuster [Israël] ; Adi Avni [Israël]Source :
- The Plant journal : for cell and molecular biology [ 1365-313X ] ; 2020.
Abstract
The first line of plant defense occurs when a plant pattern recognition receptor (PRR) recognizes microbe-associated molecular patterns. Plant PRRs are either receptor-like kinases (RLKs), which have an extracellular domain for ligand binding, a single-pass transmembrane domain, and an intracellular kinase domain for activating downstream signaling, or receptor-like proteins (RLPs), which share the same overall structure but lack an intracellular kinase domain. The tomato (Solanum lycopersicum) LeEIX2 is an RLP that binds ethylene-inducing xylanase (EIX), a fungal elicitor. To identify LeEIX2 receptor interactors, we conducted a yeast two-hybrid screen and found a tomato protein that we termed SlRLK-like. The interaction of LeEIX2 with SlRLK-like was verified using co-immunoprecipitation and bimolecular fluorescence complementation assays. The defense responses induced by EIX were markedly reduced when SlRLK-like was overexpressed in Nicotiana benthamiana or Nicotiana tabacum, and knockout of SlRLK-like using the CRISPR/Cas9 system increased EIX-induced ethylene production and 1-aminocyclopropane-1-carboxylate synthase (SlACS2) gene expression in tomato. Co-expression of SlRLK-like with LeEIX2 led to a reduction in its abundance, apparently through an endoplasmic reticulum-associated degradation process. Notably, truncation of SlRLK-like protein revealed that the malectin-like domain is sufficient and essential for its function. Moreover, SlRLK-like associated with the RLK FLS2, resulting in its degradation and concomitantly a reduction of the flagellin 22 (flg22)-induced burst of reactive oxygen species. In addition, SlRLK-like co-expression with other RLPs, Ve1 and AtRLP23, also led to a reduction in their abundance. Our findings suggest that SlRLK-like leads to a decreased stability of various PRRs, leading to a reduction in their abundance and resulting in attenuation of defense responses.
DOI: 10.1111/tpj.15006
PubMed: 33048397
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EIX-induced immune responses.</title><author><name sortKey="Sussholz, Orian" sort="Sussholz, Orian" uniqKey="Sussholz O" first="Orian" last="Sussholz">Orian Sussholz</name><affiliation wicri:level="1"><nlm:affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978</wicri:regionArea><wicri:noRegion>69978</wicri:noRegion></affiliation></author><author><name sortKey="Pizarro, Lorena" sort="Pizarro, Lorena" uniqKey="Pizarro L" first="Lorena" last="Pizarro">Lorena Pizarro</name><affiliation wicri:level="1"><nlm:affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978</wicri:regionArea><wicri:noRegion>69978</wicri:noRegion></affiliation></author><author><name sortKey="Schuster, Silvia" sort="Schuster, Silvia" uniqKey="Schuster S" first="Silvia" last="Schuster">Silvia Schuster</name><affiliation wicri:level="1"><nlm:affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978</wicri:regionArea><wicri:noRegion>69978</wicri:noRegion></affiliation></author><author><name sortKey="Avni, Adi" sort="Avni, Adi" uniqKey="Avni A" first="Adi" last="Avni">Adi Avni</name><affiliation wicri:level="1"><nlm:affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</nlm:affiliation><country xml:lang="fr">Israël</country><wicri:regionArea>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978</wicri:regionArea><wicri:noRegion>69978</wicri:noRegion></affiliation></author></analytic><series><title level="j">The Plant journal : for cell and molecular biology</title><idno type="eISSN">1365-313X</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 first line of plant defense occurs when a plant pattern recognition receptor (PRR) recognizes microbe-associated molecular patterns. Plant PRRs are either receptor-like kinases (RLKs), which have an extracellular domain for ligand binding, a single-pass transmembrane domain, and an intracellular kinase domain for activating downstream signaling, or receptor-like proteins (RLPs), which share the same overall structure but lack an intracellular kinase domain. The tomato (Solanum lycopersicum) LeEIX2 is an RLP that binds ethylene-inducing xylanase (EIX), a fungal elicitor. To identify LeEIX2 receptor interactors, we conducted a yeast two-hybrid screen and found a tomato protein that we termed SlRLK-like. The interaction of LeEIX2 with SlRLK-like was verified using co-immunoprecipitation and bimolecular fluorescence complementation assays. The defense responses induced by EIX were markedly reduced when SlRLK-like was overexpressed in Nicotiana benthamiana or Nicotiana tabacum, and knockout of SlRLK-like using the CRISPR/Cas9 system increased EIX-induced ethylene production and 1-aminocyclopropane-1-carboxylate synthase (SlACS2) gene expression in tomato. Co-expression of SlRLK-like with LeEIX2 led to a reduction in its abundance, apparently through an endoplasmic reticulum-associated degradation process. Notably, truncation of SlRLK-like protein revealed that the malectin-like domain is sufficient and essential for its function. Moreover, SlRLK-like associated with the RLK FLS2, resulting in its degradation and concomitantly a reduction of the flagellin 22 (flg22)-induced burst of reactive oxygen species. In addition, SlRLK-like co-expression with other RLPs, Ve1 and AtRLP23, also led to a reduction in their abundance. Our findings suggest that SlRLK-like leads to a decreased stability of various PRRs, leading to a reduction in their abundance and resulting in attenuation of defense responses.</div></front></TEI><pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">33048397</PMID><DateRevised><Year>2020</Year><Month>10</Month><Day>23</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1365-313X</ISSN><JournalIssue CitedMedium="Internet"><PubDate><Year>2020</Year><Month>Oct</Month><Day>13</Day></PubDate></JournalIssue><Title>The Plant journal : for cell and molecular biology</Title><ISOAbbreviation>Plant J</ISOAbbreviation></Journal><ArticleTitle>SlRLK-like is a malectin-like domain protein affecting localization and abundance of LeEIX2 receptor resulting in suppression of EIX-induced immune responses.</ArticleTitle><ELocationID EIdType="doi" ValidYN="Y">10.1111/tpj.15006</ELocationID><Abstract><AbstractText>The first line of plant defense occurs when a plant pattern recognition receptor (PRR) recognizes microbe-associated molecular patterns. Plant PRRs are either receptor-like kinases (RLKs), which have an extracellular domain for ligand binding, a single-pass transmembrane domain, and an intracellular kinase domain for activating downstream signaling, or receptor-like proteins (RLPs), which share the same overall structure but lack an intracellular kinase domain. The tomato (Solanum lycopersicum) LeEIX2 is an RLP that binds ethylene-inducing xylanase (EIX), a fungal elicitor. To identify LeEIX2 receptor interactors, we conducted a yeast two-hybrid screen and found a tomato protein that we termed SlRLK-like. The interaction of LeEIX2 with SlRLK-like was verified using co-immunoprecipitation and bimolecular fluorescence complementation assays. The defense responses induced by EIX were markedly reduced when SlRLK-like was overexpressed in Nicotiana benthamiana or Nicotiana tabacum, and knockout of SlRLK-like using the CRISPR/Cas9 system increased EIX-induced ethylene production and 1-aminocyclopropane-1-carboxylate synthase (SlACS2) gene expression in tomato. Co-expression of SlRLK-like with LeEIX2 led to a reduction in its abundance, apparently through an endoplasmic reticulum-associated degradation process. Notably, truncation of SlRLK-like protein revealed that the malectin-like domain is sufficient and essential for its function. Moreover, SlRLK-like associated with the RLK FLS2, resulting in its degradation and concomitantly a reduction of the flagellin 22 (flg22)-induced burst of reactive oxygen species. In addition, SlRLK-like co-expression with other RLPs, Ve1 and AtRLP23, also led to a reduction in their abundance. Our findings suggest that SlRLK-like leads to a decreased stability of various PRRs, leading to a reduction in their abundance and resulting in attenuation of defense responses.</AbstractText><CopyrightInformation>© 2020 Society for Experimental Biology and John Wiley & Sons Ltd.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sussholz</LastName><ForeName>Orian</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pizarro</LastName><ForeName>Lorena</ForeName><Initials>L</Initials><Identifier Source="ORCID">https://orcid.org/0000-0001-5954-5839</Identifier><AffiliationInfo><Affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schuster</LastName><ForeName>Silvia</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Avni</LastName><ForeName>Adi</ForeName><Initials>A</Initials><Identifier Source="ORCID">https://orcid.org/0000-0003-2092-9768</Identifier><AffiliationInfo><Affiliation>School of Plant Sciences and Food Security, Tel Aviv University, Tel Aviv, 69978, Israel.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>2013227</GrantID><Agency>United States-Israel Binational Science Foundation</Agency><Country></Country></Grant><Grant><GrantID>550/18</GrantID><Agency>Israel Science Foundation administered by the Israel Academy of Science and Humanities</Agency><Country></Country></Grant><Grant><GrantID>IS-4842-15 R</GrantID><Agency>United States - Israel Binational Agricultural Research and Development Fund</Agency><Country></Country></Grant><Grant><GrantID>13-37-0001</GrantID><Agency>Chief Scientist of the Israel Ministry of Agriculture and Rural Development</Agency><Country></Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>10</Month><Day>13</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Plant J</MedlineTA><NlmUniqueID>9207397</NlmUniqueID><ISSNLinking>0960-7412</ISSNLinking></MedlineJournalInfo><CitationSubset>IM</CitationSubset><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">malectin-like domain</Keyword><Keyword MajorTopicYN="N">pattern recognition receptor</Keyword><Keyword MajorTopicYN="N">plant immunity receptor-like kinase</Keyword><Keyword MajorTopicYN="N">receptor-like protein</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>06</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>09</Month><Day>05</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>09</Month><Day>15</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>10</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>10</Month><Day>13</Day><Hour>12</Hour><Minute>15</Minute></PubMedPubDate></History><PublicationStatus>aheadofprint</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">33048397</ArticleId><ArticleId IdType="doi">10.1111/tpj.15006</ArticleId></ArticleIdList><ReferenceList><Title>References</Title><Reference><Citation>Albert, I., Böhm, H., Albert, M. et al. 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Trends Immunol. 35, 345-351.</Citation></Reference></ReferenceList></PubmedData></pubmed><affiliations><list><country><li>Israël</li></country></list><tree><country name="Israël"><noRegion><name sortKey="Sussholz, Orian" sort="Sussholz, Orian" uniqKey="Sussholz O" first="Orian" last="Sussholz">Orian Sussholz</name></noRegion><name sortKey="Avni, Adi" sort="Avni, Adi" uniqKey="Avni A" first="Adi" last="Avni">Adi Avni</name><name sortKey="Pizarro, Lorena" sort="Pizarro, Lorena" uniqKey="Pizarro L" first="Lorena" last="Pizarro">Lorena Pizarro</name><name sortKey="Schuster, Silvia" sort="Schuster, Silvia" uniqKey="Schuster S" first="Silvia" last="Schuster">Silvia Schuster</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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