Serveur d'exploration sur les récepteurs immunitaires végétaux

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Discovery of a Family of Mixed Lineage Kinase Domain-like Proteins in Plants and Their Role in Innate Immune Signaling.

Identifieur interne : 000178 ( Main/Exploration ); précédent : 000177; suivant : 000179

Discovery of a Family of Mixed Lineage Kinase Domain-like Proteins in Plants and Their Role in Innate Immune Signaling.

Auteurs : Lisa K. Mahdi [Allemagne] ; Menghang Huang [République populaire de Chine] ; Xiaoxiao Zhang [République populaire de Chine] ; Ryohei Thomas Nakano [Allemagne] ; Leïla Brulé Kopp [France] ; Isabel M L. Saur [Allemagne] ; Florence Jacob [France] ; Viera Kovacova [Allemagne] ; Dmitry Lapin [Allemagne] ; Jane E. Parker [Allemagne] ; James M. Murphy [Australie] ; Kay Hofmann [Allemagne] ; Paul Schulze-Lefert [Allemagne] ; Jijie Chai [Allemagne] ; Takaki Maekawa [Allemagne]

Source :

RBID : pubmed:33053377

Abstract

HeLo domain-containing mixed lineage kinase domain-like protein (MLKL), a pseudokinase, mediates necroptotic cell death in animals. Here, we report the discovery of a conserved protein family across seed plants that structurally resembles vertebrate MLKL. The Arabidopsis genome encodes three MLKLs (AtMLKLs) with overlapping functions in disease resistance mediated by Toll-interleukin 1-receptor domain intracellular immune receptors (TNLs). The HeLo domain of AtMLKLs confers cell death activity but is dispensable for immunity. Cryo-EM structures reveal a tetrameric configuration, in which the HeLo domain is buried, suggestive of an auto-repressed complex. The mobility of AtMLKL1 along microtubules is reduced by chitin, a fungal immunity-triggering molecule. An AtMLKL1 phosphomimetic variant exhibiting reduced mobility enhances immunity. Coupled with the predicted presence of HeLo domains in plant helper NLRs, our data reveal the importance of HeLo domain proteins for TNL-dependent immunity and argue for a cell death-independent immune mechanism mediated by MLKLs.

DOI: 10.1016/j.chom.2020.08.012
PubMed: 33053377


Affiliations:


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Le document en format XML

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<name sortKey="Huang, Menghang" sort="Huang, Menghang" uniqKey="Huang M" first="Menghang" last="Huang">Menghang Huang</name>
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<name sortKey="Zhang, Xiaoxiao" sort="Zhang, Xiaoxiao" uniqKey="Zhang X" first="Xiaoxiao" last="Zhang">Xiaoxiao Zhang</name>
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<nlm:affiliation>Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany; Cluster of Excellence on Plant Sciences (CEPLAS), Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.</nlm:affiliation>
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<name sortKey="Chai, Jijie" sort="Chai, Jijie" uniqKey="Chai J" first="Jijie" last="Chai">Jijie Chai</name>
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<nlm:affiliation>Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany; Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, Center for Plant Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China; Cluster of Excellence on Plant Sciences (CEPLAS), Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.</nlm:affiliation>
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<name sortKey="Maekawa, Takaki" sort="Maekawa, Takaki" uniqKey="Maekawa T" first="Takaki" last="Maekawa">Takaki Maekawa</name>
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<title level="j">Cell host & microbe</title>
<idno type="eISSN">1934-6069</idno>
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<div type="abstract" xml:lang="en">HeLo domain-containing mixed lineage kinase domain-like protein (MLKL), a pseudokinase, mediates necroptotic cell death in animals. Here, we report the discovery of a conserved protein family across seed plants that structurally resembles vertebrate MLKL. The Arabidopsis genome encodes three MLKLs (AtMLKLs) with overlapping functions in disease resistance mediated by Toll-interleukin 1-receptor domain intracellular immune receptors (TNLs). The HeLo domain of AtMLKLs confers cell death activity but is dispensable for immunity. Cryo-EM structures reveal a tetrameric configuration, in which the HeLo domain is buried, suggestive of an auto-repressed complex. The mobility of AtMLKL1 along microtubules is reduced by chitin, a fungal immunity-triggering molecule. An AtMLKL1 phosphomimetic variant exhibiting reduced mobility enhances immunity. Coupled with the predicted presence of HeLo domains in plant helper NLRs, our data reveal the importance of HeLo domain proteins for TNL-dependent immunity and argue for a cell death-independent immune mechanism mediated by MLKLs.</div>
</front>
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<Year>2020</Year>
<Month>10</Month>
<Day>14</Day>
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<Year>2020</Year>
<Month>Sep</Month>
<Day>30</Day>
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<Title>Cell host & microbe</Title>
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<ArticleTitle>Discovery of a Family of Mixed Lineage Kinase Domain-like Proteins in Plants and Their Role in Innate Immune Signaling.</ArticleTitle>
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<AbstractText>HeLo domain-containing mixed lineage kinase domain-like protein (MLKL), a pseudokinase, mediates necroptotic cell death in animals. Here, we report the discovery of a conserved protein family across seed plants that structurally resembles vertebrate MLKL. The Arabidopsis genome encodes three MLKLs (AtMLKLs) with overlapping functions in disease resistance mediated by Toll-interleukin 1-receptor domain intracellular immune receptors (TNLs). The HeLo domain of AtMLKLs confers cell death activity but is dispensable for immunity. Cryo-EM structures reveal a tetrameric configuration, in which the HeLo domain is buried, suggestive of an auto-repressed complex. The mobility of AtMLKL1 along microtubules is reduced by chitin, a fungal immunity-triggering molecule. An AtMLKL1 phosphomimetic variant exhibiting reduced mobility enhances immunity. Coupled with the predicted presence of HeLo domains in plant helper NLRs, our data reveal the importance of HeLo domain proteins for TNL-dependent immunity and argue for a cell death-independent immune mechanism mediated by MLKLs.</AbstractText>
<CopyrightInformation>Copyright © 2020 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
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<Author ValidYN="Y">
<LastName>Mahdi</LastName>
<ForeName>Lisa K</ForeName>
<Initials>LK</Initials>
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<Affiliation>Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.</Affiliation>
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<Author ValidYN="Y">
<LastName>Huang</LastName>
<ForeName>Menghang</ForeName>
<Initials>M</Initials>
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<Affiliation>Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, Center for Plant Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.</Affiliation>
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<ForeName>Xiaoxiao</ForeName>
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<Affiliation>Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, Center for Plant Biology, School of Life Sciences, Tsinghua University, 100084 Beijing, China.</Affiliation>
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</Author>
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<ForeName>Ryohei Thomas</ForeName>
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<Affiliation>Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany; Cluster of Excellence on Plant Sciences (CEPLAS), Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany.</Affiliation>
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<ForeName>Leïla Brulé</ForeName>
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<Affiliation>Max Planck Institute for Plant Breeding Research, 50829 Cologne, Germany; Institute of Plant Sciences Paris-Saclay, Centre National de la Recherche Scientifique, Institut National de la Recherche Agronomique, Université Paris Sud, Université d'Evry, Université Paris Diderot, Sorbonne Paris-Cité, Université Paris-Saclay, 91405 Orsay, France.</Affiliation>
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<Year>2020</Year>
<Month>09</Month>
<Day>30</Day>
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<Country>United States</Country>
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<Keyword MajorTopicYN="N">Cell death</Keyword>
<Keyword MajorTopicYN="N">HeLo domain</Keyword>
<Keyword MajorTopicYN="N">MLKL</Keyword>
<Keyword MajorTopicYN="N">cryo-electron microscopy structures</Keyword>
<Keyword MajorTopicYN="N">microtubules</Keyword>
<Keyword MajorTopicYN="N">necroptosis</Keyword>
<Keyword MajorTopicYN="N">toll-interleukin1-receptor domain intracellular immune receptors</Keyword>
</KeywordList>
<CoiStatement>Declaration of Interests The authors declare no competing interests.</CoiStatement>
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