SUSA2 is an F-box protein required for autoimmunity mediated by paired NLRs SOC3-CHS1 and SOC3-TN2.
Identifieur interne : 000058 ( Main/Exploration ); précédent : 000057; suivant : 000059SUSA2 is an F-box protein required for autoimmunity mediated by paired NLRs SOC3-CHS1 and SOC3-TN2.
Auteurs : Wanwan Liang [Canada] ; Meixuezi Tong [Canada] ; Xin Li [Canada]Source :
- Nature communications [ 2041-1723 ] ; 2020.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Arabidopsis, Protéines F-box, Protéines NLR, Protéines d'Arabidopsis, Récepteurs immunologiques, Ubiquitin-protein ligases.
- physiologie : Auto-immunité, Immunité des plantes.
- Ubiquitination.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Arabidopsis Proteins, F-Box Proteins, NLR Proteins, Receptors, Immunologic, Ubiquitin-Protein Ligases.
- metabolism : Arabidopsis.
- physiology : Autoimmunity, Plant Immunity.
- Ubiquitination.
Abstract
Both higher plants and mammals rely on nucleotide-binding leucine-rich repeat (NLR) immune receptors to detect pathogens and initiate immunity. Upon effector recognition, plant NLRs oligomerize for defense activation, the mechanism of which is poorly understood. We previously showed that disruption of the E3 ligase, Senescence-Associated E3 Ubiquitin Ligase 1 (SAUL1) leads to the activation of the NLR SOC3. Here, we report the identification of suppressor of saul1 2 (susa2) and susa3 from the saul1-1 suppressor screen. Pairwise interaction analysis suggests that both SUSA proteins interact with components of an SCFSUSA2 E3 ligase complex as well as CHS1 or TN2, truncated NLRs that pair with SOC3. susa2-2 only suppresses the autoimmunity mediated by either CHS1 or TN2, suggesting its specific involvement in SOC3-mediated immunity. In summary, our study indicates links between plant NLRs and an SCF complex that may enable ubiquitination and degradation of unknown downstream components to activate defense.
DOI: 10.1038/s41467-020-19033-z
PubMed: 33060601
PubMed Central: PMC7562919
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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type="state">Colombie-Britannique </region></placeName></affiliation></author></analytic><series><title level="j">Nature communications</title><idno type="eISSN">2041-1723</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Arabidopsis (metabolism)</term><term>Arabidopsis Proteins (metabolism)</term><term>Autoimmunity (physiology)</term><term>F-Box Proteins (metabolism)</term><term>NLR Proteins (metabolism)</term><term>Plant Immunity (physiology)</term><term>Receptors, Immunologic (metabolism)</term><term>Ubiquitin-Protein Ligases (metabolism)</term><term>Ubiquitination (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Arabidopsis (métabolisme)</term><term>Auto-immunité (physiologie)</term><term>Immunité des plantes (physiologie)</term><term>Protéines F-box (métabolisme)</term><term>Protéines NLR (métabolisme)</term><term>Protéines d'Arabidopsis (métabolisme)</term><term>Récepteurs immunologiques (métabolisme)</term><term>Ubiquitin-protein ligases (métabolisme)</term><term>Ubiquitination (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Arabidopsis Proteins</term><term>F-Box Proteins</term><term>NLR Proteins</term><term>Receptors, Immunologic</term><term>Ubiquitin-Protein Ligases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Arabidopsis</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Arabidopsis</term><term>Protéines F-box</term><term>Protéines NLR</term><term>Protéines d'Arabidopsis</term><term>Récepteurs immunologiques</term><term>Ubiquitin-protein ligases</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Auto-immunité</term><term>Immunité des plantes</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Autoimmunity</term><term>Plant Immunity</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Ubiquitination</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Both higher plants and mammals rely on nucleotide-binding leucine-rich repeat (NLR) immune receptors to detect pathogens and initiate immunity. Upon effector recognition, plant NLRs oligomerize for defense activation, the mechanism of which is poorly understood. We previously showed that disruption of the E3 ligase, Senescence-Associated E3 Ubiquitin Ligase 1 (SAUL1) leads to the activation of the NLR SOC3. Here, we report the identification of suppressor of saul1 2 (susa2) and susa3 from the saul1-1 suppressor screen. Pairwise interaction analysis suggests that both SUSA proteins interact with components of an SCF<sup>SUSA2</sup> E3 ligase complex as well as CHS1 or TN2, truncated NLRs that pair with SOC3. susa2-2 only suppresses the autoimmunity mediated by either CHS1 or TN2, suggesting its specific involvement in SOC3-mediated immunity. In summary, our study indicates links between plant NLRs and an SCF complex that may enable ubiquitination and degradation of unknown downstream components to activate defense.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">33060601</PMID><DateCompleted><Year>2020</Year><Month>11</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>11</Month><Day>02</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">2041-1723</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>1</Issue><PubDate><Year>2020</Year><Month>10</Month><Day>15</Day></PubDate></JournalIssue><Title>Nature communications</Title><ISOAbbreviation>Nat Commun</ISOAbbreviation></Journal><ArticleTitle>SUSA2 is an F-box protein required for autoimmunity mediated by paired NLRs SOC3-CHS1 and SOC3-TN2.</ArticleTitle><Pagination><MedlinePgn>5190</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/s41467-020-19033-z</ELocationID><Abstract><AbstractText>Both higher plants and mammals rely on nucleotide-binding leucine-rich repeat (NLR) immune receptors to detect pathogens and initiate immunity. Upon effector recognition, plant NLRs oligomerize for defense activation, the mechanism of which is poorly understood. We previously showed that disruption of the E3 ligase, Senescence-Associated E3 Ubiquitin Ligase 1 (SAUL1) leads to the activation of the NLR SOC3. Here, we report the identification of suppressor of saul1 2 (susa2) and susa3 from the saul1-1 suppressor screen. Pairwise interaction analysis suggests that both SUSA proteins interact with components of an SCF<sup>SUSA2</sup> E3 ligase complex as well as CHS1 or TN2, truncated NLRs that pair with SOC3. susa2-2 only suppresses the autoimmunity mediated by either CHS1 or TN2, suggesting its specific involvement in SOC3-mediated immunity. In summary, our study indicates links between plant NLRs and an SCF complex that may enable ubiquitination and degradation of unknown downstream components to activate defense.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Liang</LastName><ForeName>Wanwan</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Michael Smith Laboratories, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Botany, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tong</LastName><ForeName>Meixuezi</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Michael Smith Laboratories, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Botany, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Xin</ForeName><Initials>X</Initials><Identifier Source="ORCID">0000-0002-6354-2021</Identifier><AffiliationInfo><Affiliation>Michael Smith Laboratories, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada. xinli@msl.ubc.ca.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Department of Botany, University of British Columbia, Vancouver, BC, V6T 1Z4, Canada. xinli@msl.ubc.ca.</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>10</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Nat Commun</MedlineTA><NlmUniqueID>101528555</NlmUniqueID><ISSNLinking>2041-1723</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C120363">ASK1 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D029681">Arabidopsis Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C587982">CHS1 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D044783">F-Box Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000070576">NLR Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011971">Receptors, Immunologic</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C000627024">SOC3 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance UI="C576658">SAUL1 protein, Arabidopsis</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.3.2.27</RegistryNumber><NameOfSubstance UI="D044767">Ubiquitin-Protein Ligases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D017360" MajorTopicYN="N">Arabidopsis</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029681" MajorTopicYN="N">Arabidopsis Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015551" MajorTopicYN="N">Autoimmunity</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044783" MajorTopicYN="N">F-Box Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000070576" MajorTopicYN="N">NLR Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D057865" MajorTopicYN="N">Plant Immunity</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011971" MajorTopicYN="N">Receptors, Immunologic</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D044767" MajorTopicYN="N">Ubiquitin-Protein Ligases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054875" 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</li></region><settlement><li>Vancouver</li></settlement><orgName><li>Université de la Colombie-Britannique</li></orgName></list><tree><country name="Canada"><region name="Colombie-Britannique "><name sortKey="Liang, Wanwan" sort="Liang, Wanwan" uniqKey="Liang W" first="Wanwan" last="Liang">Wanwan Liang</name></region><name sortKey="Li, Xin" sort="Li, Xin" uniqKey="Li X" first="Xin" last="Li">Xin Li</name><name sortKey="Li, Xin" sort="Li, Xin" uniqKey="Li X" first="Xin" last="Li">Xin Li</name><name sortKey="Liang, Wanwan" sort="Liang, Wanwan" uniqKey="Liang W" first="Wanwan" last="Liang">Wanwan Liang</name><name sortKey="Tong, Meixuezi" sort="Tong, Meixuezi" uniqKey="Tong M" first="Meixuezi" last="Tong">Meixuezi Tong</name><name sortKey="Tong, Meixuezi" sort="Tong, Meixuezi" uniqKey="Tong M" first="Meixuezi" last="Tong">Meixuezi Tong</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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