Disruption of PAMP-Induced MAP Kinase Cascade by a Pseudomonas syringae Effector Activates Plant Immunity Mediated by the NB-LRR Protein SUMM2
Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) serves as a primary plant defense response against microbial pathogens, with MEKK1, MKK1/MKK2, and MPK4 functioning as a MAP kinase cascade downstream of PAMP receptors. Plant Resistance (R) proteins sense specific pathogen effect...
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| Published in | Cell host & microbe Vol. 11; no. 3; pp. 253 - 263 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
15.03.2012
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) serves as a primary plant defense response against microbial pathogens, with MEKK1, MKK1/MKK2, and MPK4 functioning as a MAP kinase cascade downstream of PAMP receptors. Plant Resistance (R) proteins sense specific pathogen effectors to initiate a second defense mechanism, termed effector-triggered immunity (ETI). In a screen for suppressors of the mkk1 mkk2 autoimmune phenotype, we identify the nucleotide-binding leucine-rich repeat (NB-LRR) protein SUMM2 and find that the MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates SUMM2-mediated immunity. Further, the MEKK1-MKK1/MKK2-MPK4 cascade positively regulates basal defense targeted by the Pseudomonas syringae pathogenic effector HopAI1, which inhibits MPK4 kinase activity. Inactivation of MPK4 by HopAI1 results in activation of SUMM2-mediated defense responses. Our data suggest that SUMM2 is an R protein that becomes active when the MEKK1-MKK1/MKK2-MPK4 cascade is disrupted by pathogens, supporting the hypothesis that R proteins evolved to protect plants when microbial effectors suppress basal resistance.
► The MEKK1-MKK1/MKK2-MPK4 kinase cascade is required for basal defense ► MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates NB-LRR protein SUMM2-mediated immunity ► The bacterial pathogenic effector HopAI1 targets MPK4 kinase activity ► Inactivation of MPK4 by HopAI1 activates SUMM2-mediated immune responses |
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| AbstractList | Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) serves as a primary plant defense response against microbial pathogens, with MEKK1, MKK1/MKK2, and MPK4 functioning as a MAP kinase cascade downstream of PAMP receptors. Plant Resistance (R) proteins sense specific pathogen effectors to initiate a second defense mechanism, termed effector-triggered immunity (ETI). In a screen for suppressors of the mkk1 mkk2 autoimmune phenotype, we identify the nucleotide-binding leucine-rich repeat (NB-LRR) protein SUMM2 and find that the MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates SUMM2-mediated immunity. Further, the MEKK1-MKK1/MKK2-MPK4 cascade positively regulates basal defense targeted by the Pseudomonas syringae pathogenic effector HopAI1, which inhibits MPK4 kinase activity. Inactivation of MPK4 by HopAI1 results in activation of SUMM2-mediated defense responses. Our data suggest that SUMM2 is an R protein that becomes active when the MEKK1-MKK1/MKK2-MPK4 cascade is disrupted by pathogens, supporting the hypothesis that R proteins evolved to protect plants when microbial effectors suppress basal resistance. Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) serves as a primary plant defense response against microbial pathogens, with MEKK1, MKK1/MKK2, and MPK4 functioning as a MAP kinase cascade downstream of PAMP receptors. Plant Resistance (R) proteins sense specific pathogen effectors to initiate a second defense mechanism, termed effector-triggered immunity (ETI). In a screen for suppressors of the mkk1 mkk2 autoimmune phenotype, we identify the nucleotide-binding leucine-rich repeat (NB-LRR) protein SUMM2 and find that the MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates SUMM2-mediated immunity. Further, the MEKK1-MKK1/MKK2-MPK4 cascade positively regulates basal defense targeted by the Pseudomonas syringae pathogenic effector HopAI1, which inhibits MPK4 kinase activity. Inactivation of MPK4 by HopAI1 results in activation of SUMM2-mediated defense responses. Our data suggest that SUMM2 is an R protein that becomes active when the MEKK1-MKK1/MKK2-MPK4 cascade is disrupted by pathogens, supporting the hypothesis that R proteins evolved to protect plants when microbial effectors suppress basal resistance.Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) serves as a primary plant defense response against microbial pathogens, with MEKK1, MKK1/MKK2, and MPK4 functioning as a MAP kinase cascade downstream of PAMP receptors. Plant Resistance (R) proteins sense specific pathogen effectors to initiate a second defense mechanism, termed effector-triggered immunity (ETI). In a screen for suppressors of the mkk1 mkk2 autoimmune phenotype, we identify the nucleotide-binding leucine-rich repeat (NB-LRR) protein SUMM2 and find that the MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates SUMM2-mediated immunity. Further, the MEKK1-MKK1/MKK2-MPK4 cascade positively regulates basal defense targeted by the Pseudomonas syringae pathogenic effector HopAI1, which inhibits MPK4 kinase activity. Inactivation of MPK4 by HopAI1 results in activation of SUMM2-mediated defense responses. Our data suggest that SUMM2 is an R protein that becomes active when the MEKK1-MKK1/MKK2-MPK4 cascade is disrupted by pathogens, supporting the hypothesis that R proteins evolved to protect plants when microbial effectors suppress basal resistance. Pathogen-associated molecular pattern (PAMP)-triggered immunity (PTI) serves as a primary plant defense response against microbial pathogens, with MEKK1, MKK1/MKK2, and MPK4 functioning as a MAP kinase cascade downstream of PAMP receptors. Plant Resistance (R) proteins sense specific pathogen effectors to initiate a second defense mechanism, termed effector-triggered immunity (ETI). In a screen for suppressors of the mkk1 mkk2 autoimmune phenotype, we identify the nucleotide-binding leucine-rich repeat (NB-LRR) protein SUMM2 and find that the MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates SUMM2-mediated immunity. Further, the MEKK1-MKK1/MKK2-MPK4 cascade positively regulates basal defense targeted by the Pseudomonas syringae pathogenic effector HopAI1, which inhibits MPK4 kinase activity. Inactivation of MPK4 by HopAI1 results in activation of SUMM2-mediated defense responses. Our data suggest that SUMM2 is an R protein that becomes active when the MEKK1-MKK1/MKK2-MPK4 cascade is disrupted by pathogens, supporting the hypothesis that R proteins evolved to protect plants when microbial effectors suppress basal resistance. ► The MEKK1-MKK1/MKK2-MPK4 kinase cascade is required for basal defense ► MEKK1-MKK1/MKK2-MPK4 cascade negatively regulates NB-LRR protein SUMM2-mediated immunity ► The bacterial pathogenic effector HopAI1 targets MPK4 kinase activity ► Inactivation of MPK4 by HopAI1 activates SUMM2-mediated immune responses |
| Author | Wu, Yaling Kong, Qing Gao, Minghui Zhang, Zhibin Ba, Hongping Zhang, Jie Zhou, Jianmin Zhang, Yuelin Liu, Yanan |
| Author_xml | – sequence: 1 givenname: Zhibin surname: Zhang fullname: Zhang, Zhibin organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 2 givenname: Yaling surname: Wu fullname: Wu, Yaling organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 3 givenname: Minghui surname: Gao fullname: Gao, Minghui organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 4 givenname: Jie surname: Zhang fullname: Zhang, Jie organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 5 givenname: Qing surname: Kong fullname: Kong, Qing organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 6 givenname: Yanan surname: Liu fullname: Liu, Yanan organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 7 givenname: Hongping surname: Ba fullname: Ba, Hongping organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 8 givenname: Jianmin surname: Zhou fullname: Zhou, Jianmin organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China – sequence: 9 givenname: Yuelin surname: Zhang fullname: Zhang, Yuelin email: yuelin.zhang@ubc.ca organization: National Institute of Biological Sciences, Zhongguancun Life Science Park, Number 7 Science Park Road, Beijing 102206, People's Republic of China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/22423965$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Alleles Arabidopsis - immunology Arabidopsis - metabolism Arabidopsis - microbiology Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis Proteins - physiology Bacterial Proteins - immunology Bacterial Proteins - metabolism Carrier Proteins - genetics Carrier Proteins - metabolism Carrier Proteins - physiology Cell Death DNA Mutational Analysis Host-Pathogen Interactions immunity MAP Kinase Signaling System mitogen-activated protein kinase Mutation, Missense pathogens phenotype Plant Diseases - immunology Plant Diseases - microbiology Plant Immunity Protein Kinases - genetics Protein Kinases - metabolism Protein Structure, Tertiary Pseudomonas syringae Pseudomonas syringae - physiology receptors Receptors, Pattern Recognition - metabolism |
| Title | Disruption of PAMP-Induced MAP Kinase Cascade by a Pseudomonas syringae Effector Activates Plant Immunity Mediated by the NB-LRR Protein SUMM2 |
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