Functional roles of the pepper leucine-rich repeat protein and its interactions with pathogenesis-related and hypersensitive-induced proteins in plant cell death and immunity.
Identifieur interne : 000237 ( Main/Exploration ); précédent : 000236; suivant : 000238Functional roles of the pepper leucine-rich repeat protein and its interactions with pathogenesis-related and hypersensitive-induced proteins in plant cell death and immunity.
Auteurs : Jeum Kyu Hong [Corée du Sud] ; In Sun Hwang [Corée du Sud] ; Byung Kook Hwang [Corée du Sud]Source :
- Planta [ 1432-2048 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
- génétique : Capsicum, Immunité des plantes, Mort cellulaire, Protéines, Protéines végétales.
- métabolisme : Capsicum.
- physiologie : Protéines, Protéines végétales.
- Maladies des plantes.
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Plant Proteins, Proteins.
- genetics : Capsicum, Cell Death, Plant Immunity.
- metabolism : Capsicum.
- chemical , physiology : Plant Proteins, Proteins.
- Plant Diseases.
Abstract
MAIN CONCLUSION
Pepper leucine-rich repeat protein (CaLRR1) interacts with defense response proteins to regulate plant cell death and immunity. This review highlights the current understanding of the molecular functions of CaLRR1 and its interactor proteins. Plant cell death and immune responses to microbial pathogens are controlled by complex and tightly regulated molecular signaling networks. Xanthomonas campestris pv. vesicatoria (Xcv)-inducible pepper (Capsicum annuum) leucine-rich repeat protein 1 (CaLRR1) serves as a molecular marker for plant cell death and immunity signaling. In this review, we discuss recent advances in elucidating the functional roles of CaLRR1 and its interacting plant proteins, and understanding how they are involved in the cell death and defense responses. CaLRR1 physically interacts with pepper pathogenesis-related proteins (CaPR10 and CaPR4b) and hypersensitive-induced reaction protein (CaHIR1) to regulate plant cell death and defense responses. CaLRR1 is produced in the cytoplasm and trafficked to the extracellular matrix. CaLRR1 binds to CaPR10 in the cytoplasm and CaPR4b and CaHIR1 at the plasma membrane. CaLRR1 synergistically accelerates CaPR10-triggered hypersensitive cell death, but negatively regulates CaPR4b- and CaHIR1-triggered cell death. CaHIR1 interacts with Xcv filamentous hemagglutinin (Fha1) to trigger disease-associated cell death. The subcellular localization and cellular function of these CaLRR1 interactors during plant cell death and defense responses were elucidated by Agrobacterium-mediated transient expression, virus-induced gene silencing, and transgenic overexpression studies. CaPR10, CaPR4b, and CaHIR1 positively regulate defense signaling mediated by salicylic acid and reactive oxygen species, thereby activating hypersensitive cell death and disease resistance. A comprehensive understanding of the molecular functions of CaLRR1 and its interacting protein partners in cell death and defense responses will provide valuable information for the molecular genetics of plant disease resistance, which could be exploited as a sustainable disease management strategy.
DOI: 10.1007/s00425-017-2709-5
PubMed: 28508261
Affiliations:
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sort="Hwang, In Sun" uniqKey="Hwang I" first="In Sun" last="Hwang">In Sun Hwang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Horticultural Biotechnology, Kyung Hee University, Yongin, 17104, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Horticultural Biotechnology, Kyung Hee University, Yongin, 17104</wicri:regionArea><wicri:noRegion>17104</wicri:noRegion></affiliation></author><author><name sortKey="Hwang, Byung Kook" sort="Hwang, Byung Kook" uniqKey="Hwang B" first="Byung Kook" last="Hwang">Byung Kook Hwang</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Seoul, 02841, Republic of Korea. bkhwang@korea.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, 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Kyu" last="Hong">Jeum Kyu Hong</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Plant Pathology and Protection, Department of Horticultural Science, College of Biosciences, Gyeongnam National University of Science and Technology, Jinju, 52725, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Laboratory of Plant Pathology and Protection, Department of Horticultural Science, College of Biosciences, Gyeongnam National University of Science and Technology, Jinju, 52725</wicri:regionArea><wicri:noRegion>52725</wicri:noRegion></affiliation></author><author><name sortKey="Hwang, In Sun" sort="Hwang, In Sun" uniqKey="Hwang I" first="In Sun" last="Hwang">In Sun Hwang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Horticultural Biotechnology, Kyung Hee University, Yongin, 17104, Republic of Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Department of Horticultural Biotechnology, Kyung Hee University, Yongin, 17104</wicri:regionArea><wicri:noRegion>17104</wicri:noRegion></affiliation></author><author><name sortKey="Hwang, Byung Kook" sort="Hwang, Byung Kook" uniqKey="Hwang B" first="Byung Kook" last="Hwang">Byung Kook Hwang</name><affiliation wicri:level="1"><nlm:affiliation>Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Seoul, 02841, Republic of Korea. bkhwang@korea.ac.kr.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Seoul, 02841</wicri:regionArea><wicri:noRegion>02841</wicri:noRegion></affiliation></author></analytic><series><title level="j">Planta</title><idno type="eISSN">1432-2048</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Capsicum (genetics)</term><term>Capsicum (metabolism)</term><term>Cell Death (genetics)</term><term>Plant Diseases (MeSH)</term><term>Plant Immunity (genetics)</term><term>Plant Proteins (genetics)</term><term>Plant Proteins (physiology)</term><term>Proteins (genetics)</term><term>Proteins (physiology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Capsicum (génétique)</term><term>Capsicum (métabolisme)</term><term>Immunité des plantes (génétique)</term><term>Maladies des plantes (MeSH)</term><term>Mort cellulaire (génétique)</term><term>Protéines (génétique)</term><term>Protéines (physiologie)</term><term>Protéines végétales (génétique)</term><term>Protéines végétales (physiologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Plant Proteins</term><term>Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Capsicum</term><term>Cell Death</term><term>Plant Immunity</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Capsicum</term><term>Immunité des plantes</term><term>Mort cellulaire</term><term>Protéines</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Capsicum</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Capsicum</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Protéines</term><term>Protéines végétales</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Plant Proteins</term><term>Proteins</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Plant Diseases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Maladies des plantes</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>MAIN CONCLUSION</b></p><p>Pepper leucine-rich repeat protein (CaLRR1) interacts with defense response proteins to regulate plant cell death and immunity. This review highlights the current understanding of the molecular functions of CaLRR1 and its interactor proteins. Plant cell death and immune responses to microbial pathogens are controlled by complex and tightly regulated molecular signaling networks. Xanthomonas campestris pv. vesicatoria (Xcv)-inducible pepper (Capsicum annuum) leucine-rich repeat protein 1 (CaLRR1) serves as a molecular marker for plant cell death and immunity signaling. In this review, we discuss recent advances in elucidating the functional roles of CaLRR1 and its interacting plant proteins, and understanding how they are involved in the cell death and defense responses. CaLRR1 physically interacts with pepper pathogenesis-related proteins (CaPR10 and CaPR4b) and hypersensitive-induced reaction protein (CaHIR1) to regulate plant cell death and defense responses. CaLRR1 is produced in the cytoplasm and trafficked to the extracellular matrix. CaLRR1 binds to CaPR10 in the cytoplasm and CaPR4b and CaHIR1 at the plasma membrane. CaLRR1 synergistically accelerates CaPR10-triggered hypersensitive cell death, but negatively regulates CaPR4b- and CaHIR1-triggered cell death. CaHIR1 interacts with Xcv filamentous hemagglutinin (Fha1) to trigger disease-associated cell death. The subcellular localization and cellular function of these CaLRR1 interactors during plant cell death and defense responses were elucidated by Agrobacterium-mediated transient expression, virus-induced gene silencing, and transgenic overexpression studies. CaPR10, CaPR4b, and CaHIR1 positively regulate defense signaling mediated by salicylic acid and reactive oxygen species, thereby activating hypersensitive cell death and disease resistance. A comprehensive understanding of the molecular functions of CaLRR1 and its interacting protein partners in cell death and defense responses will provide valuable information for the molecular genetics of plant disease resistance, which could be exploited as a sustainable disease management strategy.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28508261</PMID><DateCompleted><Year>2018</Year><Month>08</Month><Day>16</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-2048</ISSN><JournalIssue CitedMedium="Internet"><Volume>246</Volume><Issue>3</Issue><PubDate><Year>2017</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Planta</Title><ISOAbbreviation>Planta</ISOAbbreviation></Journal><ArticleTitle>Functional roles of the pepper leucine-rich repeat protein and its interactions with pathogenesis-related and hypersensitive-induced proteins in plant cell death and immunity.</ArticleTitle><Pagination><MedlinePgn>351-364</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00425-017-2709-5</ELocationID><Abstract><AbstractText Label="MAIN CONCLUSION" NlmCategory="UNASSIGNED">Pepper leucine-rich repeat protein (CaLRR1) interacts with defense response proteins to regulate plant cell death and immunity. This review highlights the current understanding of the molecular functions of CaLRR1 and its interactor proteins. Plant cell death and immune responses to microbial pathogens are controlled by complex and tightly regulated molecular signaling networks. Xanthomonas campestris pv. vesicatoria (Xcv)-inducible pepper (Capsicum annuum) leucine-rich repeat protein 1 (CaLRR1) serves as a molecular marker for plant cell death and immunity signaling. In this review, we discuss recent advances in elucidating the functional roles of CaLRR1 and its interacting plant proteins, and understanding how they are involved in the cell death and defense responses. CaLRR1 physically interacts with pepper pathogenesis-related proteins (CaPR10 and CaPR4b) and hypersensitive-induced reaction protein (CaHIR1) to regulate plant cell death and defense responses. CaLRR1 is produced in the cytoplasm and trafficked to the extracellular matrix. CaLRR1 binds to CaPR10 in the cytoplasm and CaPR4b and CaHIR1 at the plasma membrane. CaLRR1 synergistically accelerates CaPR10-triggered hypersensitive cell death, but negatively regulates CaPR4b- and CaHIR1-triggered cell death. CaHIR1 interacts with Xcv filamentous hemagglutinin (Fha1) to trigger disease-associated cell death. The subcellular localization and cellular function of these CaLRR1 interactors during plant cell death and defense responses were elucidated by Agrobacterium-mediated transient expression, virus-induced gene silencing, and transgenic overexpression studies. CaPR10, CaPR4b, and CaHIR1 positively regulate defense signaling mediated by salicylic acid and reactive oxygen species, thereby activating hypersensitive cell death and disease resistance. A comprehensive understanding of the molecular functions of CaLRR1 and its interacting protein partners in cell death and defense responses will provide valuable information for the molecular genetics of plant disease resistance, which could be exploited as a sustainable disease management strategy.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Hong</LastName><ForeName>Jeum Kyu</ForeName><Initials>JK</Initials><AffiliationInfo><Affiliation>Laboratory of Plant Pathology and Protection, Department of Horticultural Science, College of Biosciences, Gyeongnam National University of Science and Technology, Jinju, 52725, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>In Sun</ForeName><Initials>IS</Initials><AffiliationInfo><Affiliation>Department of Horticultural Biotechnology, Kyung Hee University, Yongin, 17104, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hwang</LastName><ForeName>Byung Kook</ForeName><Initials>BK</Initials><Identifier Source="ORCID">http://orcid.org/0000-0003-1782-8990</Identifier><AffiliationInfo><Affiliation>Laboratory of Molecular Plant Pathology, College of Life Sciences and Biotechnology, Korea University, Seoul, 02841, Republic of Korea. bkhwang@korea.ac.kr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>05</Month><Day>15</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Planta</MedlineTA><NlmUniqueID>1250576</NlmUniqueID><ISSNLinking>0032-0935</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010940">Plant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C107657">leucine-rich repeat proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002212" MajorTopicYN="N">Capsicum</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016923" MajorTopicYN="N">Cell Death</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010935" MajorTopicYN="N">Plant Diseases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057865" MajorTopicYN="N">Plant Immunity</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010940" MajorTopicYN="N">Plant Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Cell death</Keyword><Keyword MajorTopicYN="N">Defense response</Keyword><Keyword MajorTopicYN="N">Leucine-rich repeat (LRR) protein</Keyword><Keyword MajorTopicYN="N">Pathogenesis-related (PR) protein</Keyword><Keyword MajorTopicYN="N">Pepper (Capsicum annuum)</Keyword><Keyword MajorTopicYN="N">Protein–protein interaction</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>04</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>05</Month><Day>06</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>5</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>8</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>5</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28508261</ArticleId><ArticleId IdType="doi">10.1007/s00425-017-2709-5</ArticleId><ArticleId IdType="pii">10.1007/s00425-017-2709-5</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Plant Physiol. 2009 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