Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity

In plant innate immunity, the surface‐exposed leucine‐rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen‐associated molecular patterns EF‐Tu and flagellin, respectively. We identified the Arabidopsis stromal‐derived factor‐2 (SDF2) as being required for EFR funct...

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Vydáno v:The EMBO journal Ročník 28; číslo 21; s. 3428 - 3438
Hlavní autoři: Nekrasov, Vladimir, Li, Jing, Batoux, Martine, Roux, Milena, Chu, Zhao-Hui, Lacombe, Severine, Rougon, Alejandra, Bittel, Pascal, Kiss-Papp, Marta, Chinchilla, Delphine, van Esse, H Peter, Jorda, Lucia, Schwessinger, Benjamin, Nicaise, Valerie, Thomma, Bart P H J, Molina, Antonio, Jones, Jonathan D G, Zipfel, Cyril
Médium: Journal Article
Jazyk:angličtina
Vydáno: Chichester, UK John Wiley & Sons, Ltd 04.11.2009
Nature Publishing Group UK
Springer Nature B.V
Nature Publishing Group
Témata:
agrobacterium-mediated transformation
Arabidopsis - immunology
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - immunology
Arabidopsis Proteins - metabolism
arabidopsis-thaliana
Botany
Carrier Proteins - metabolism
Catalysis
defective brassinosteroid receptor
disease resistance
EFR
EMBO30
EMBO31
Endoplasmic Reticulum - metabolism
endoplasmic-reticulum
ER-quality control
flagellin perception
HSP40 Heat-Shock Proteins - metabolism
Immunity, Innate
Immunology
innate immunity
Kinases
Molecular biology
pathogen-associated molecular patterns
Pathogens
pattern-recognition receptor
Physiology
Plant Diseases - immunology
pseudomonas-syringae
Quality control
Receptors, Pattern Recognition - genetics
Receptors, Pattern Recognition - immunology
Receptors, Pattern Recognition - metabolism
Retention
SDF2
secretory pathway
EFR
pattern‐recognition receptor
pathogen‐associated molecular patterns
SDF2
ER‐quality control
ISSN:0261-4189, 1460-2075, 1460-2075
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Abstract In plant innate immunity, the surface‐exposed leucine‐rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen‐associated molecular patterns EF‐Tu and flagellin, respectively. We identified the Arabidopsis stromal‐derived factor‐2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function. SDF2 resides in an endoplasmic reticulum (ER) protein complex with the Hsp40 ERdj3B and the Hsp70 BiP, which are components of the ER‐quality control (ER‐QC). Loss of SDF2 results in ER retention and degradation of EFR. The differential requirement for ER‐QC components by EFR and FLS2 could be linked to N‐glycosylation mediated by STT3a, a catalytic subunit of the oligosaccharyltransferase complex involved in co‐translational N‐glycosylation. Our results show that the plasma membrane EFR requires the ER complex SDF2–ERdj3B–BiP for its proper accumulation, and provide a demonstration of a physiological requirement for ER‐QC in transmembrane receptor function in plants. They also provide an unexpected differential requirement for ER‐QC and N‐glycosylation components by two closely related receptors.
AbstractList In plant innate immunity, the surface-exposed leucine-rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen-associated molecular patterns EF-Tu and flagellin, respectively. We identified the Arabidopsis stromal-derived factor-2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function. SDF2 resides in an endoplasmic reticulum (ER) protein complex with the Hsp40 ERdj3B and the Hsp70 BiP, which are components of the ER-quality control (ER-QC). Loss of SDF2 results in ER retention and degradation of EFR. The differential requirement for ER-QC components by EFR and FLS2 could be linked to N-glycosylation mediated by STT3a, a catalytic subunit of the oligosaccharyltransferase complex involved in co-translational N-glycosylation. Our results show that the plasma membrane EFR requires the ER complex SDF2-ERdj3B-BiP for its proper accumulation, and provide a demonstration of a physiological requirement for ER-QC in transmembrane receptor function in plants. They also provide an unexpected differential requirement for ER-QC and N-glycosylation components by two closely related receptors
In plant innate immunity, the surface‐exposed leucine‐rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen‐associated molecular patterns EF‐Tu and flagellin, respectively. We identified the Arabidopsis stromal‐derived factor‐2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function. SDF2 resides in an endoplasmic reticulum (ER) protein complex with the Hsp40 ERdj3B and the Hsp70 BiP, which are components of the ER‐quality control (ER‐QC). Loss of SDF2 results in ER retention and degradation of EFR. The differential requirement for ER‐QC components by EFR and FLS2 could be linked to N‐glycosylation mediated by STT3a, a catalytic subunit of the oligosaccharyltransferase complex involved in co‐translational N‐glycosylation. Our results show that the plasma membrane EFR requires the ER complex SDF2–ERdj3B–BiP for its proper accumulation, and provide a demonstration of a physiological requirement for ER‐QC in transmembrane receptor function in plants. They also provide an unexpected differential requirement for ER‐QC and N‐glycosylation components by two closely related receptors.
In plant innate immunity, the surface-exposed leucine-rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen-associated molecular patterns EF-Tu and flagellin, respectively. We identified the Arabidopsis stromal-derived factor-2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function. SDF2 resides in an endoplasmic reticulum (ER) protein complex with the Hsp40 ERdj3B and the Hsp70 BiP, which are components of the ER-quality control (ER-QC). Loss of SDF2 results in ER retention and degradation of EFR. The differential requirement for ER-QC components by EFR and FLS2 could be linked to N-glycosylation mediated by STT3a, a catalytic subunit of the oligosaccharyltransferase complex involved in co-translational N-glycosylation. Our results show that the plasma membrane EFR requires the ER complex SDF2-ERdj3B-BiP for its proper accumulation, and provide a demonstration of a physiological requirement for ER-QC in transmembrane receptor function in plants. They also provide an unexpected differential requirement for ER-QC and N-glycosylation components by two closely related receptors. [PUBLICATION ABSTRACT]
In plant innate immunity, the surface-exposed leucine-rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen-associated molecular patterns EF-Tu and flagellin, respectively. We identified the Arabidopsis stromal-derived factor-2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function. SDF2 resides in an endoplasmic reticulum (ER) protein complex with the Hsp40 ERdj3B and the Hsp70 BiP, which are components of the ER-quality control (ER-QC). Loss of SDF2 results in ER retention and degradation of EFR. The differential requirement for ER-QC components by EFR and FLS2 could be linked to N-glycosylation mediated by STT3a, a catalytic subunit of the oligosaccharyltransferase complex involved in co-translational N-glycosylation. Our results show that the plasma membrane EFR requires the ER complex SDF2-ERdj3B-BiP for its proper accumulation, and provide a demonstration of a physiological requirement for ER-QC in transmembrane receptor function in plants. They also provide an unexpected differential requirement for ER-QC and N-glycosylation components by two closely related receptors.In plant innate immunity, the surface-exposed leucine-rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen-associated molecular patterns EF-Tu and flagellin, respectively. We identified the Arabidopsis stromal-derived factor-2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function. SDF2 resides in an endoplasmic reticulum (ER) protein complex with the Hsp40 ERdj3B and the Hsp70 BiP, which are components of the ER-quality control (ER-QC). Loss of SDF2 results in ER retention and degradation of EFR. The differential requirement for ER-QC components by EFR and FLS2 could be linked to N-glycosylation mediated by STT3a, a catalytic subunit of the oligosaccharyltransferase complex involved in co-translational N-glycosylation. Our results show that the plasma membrane EFR requires the ER complex SDF2-ERdj3B-BiP for its proper accumulation, and provide a demonstration of a physiological requirement for ER-QC in transmembrane receptor function in plants. They also provide an unexpected differential requirement for ER-QC and N-glycosylation components by two closely related receptors.
Author Jones, Jonathan D G
Bittel, Pascal
Nicaise, Valerie
Kiss‐Papp, Marta
van Esse, H Peter
Jorda, Lucia
Batoux, Martine
Molina, Antonio
Li, Jing
Zipfel, Cyril
Roux, Milena
Lacombe, Severine
Nekrasov, Vladimir
Rougon, Alejandra
Thomma, Bart P H J
Chinchilla, Delphine
Chu, Zhao‐Hui
Schwessinger, Benjamin
Author_xml – sequence: 1
  givenname: Vladimir
  surname: Nekrasov
  fullname: Nekrasov, Vladimir
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 2
  givenname: Jing
  surname: Li
  fullname: Li, Jing
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 3
  givenname: Martine
  surname: Batoux
  fullname: Batoux, Martine
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 4
  givenname: Milena
  surname: Roux
  fullname: Roux, Milena
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
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  givenname: Zhao-Hui
  surname: Chu
  fullname: Chu, Zhao-Hui
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
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  givenname: Severine
  surname: Lacombe
  fullname: Lacombe, Severine
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 7
  givenname: Alejandra
  surname: Rougon
  fullname: Rougon, Alejandra
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 8
  givenname: Pascal
  surname: Bittel
  fullname: Bittel, Pascal
  organization: Basel-Zurich-Plant Science Center, Botanical Institute, University Basel, Basel, Switzerland
– sequence: 9
  givenname: Marta
  surname: Kiss-Papp
  fullname: Kiss-Papp, Marta
  organization: Basel-Zurich-Plant Science Center, Botanical Institute, University Basel, Basel, Switzerland
– sequence: 10
  givenname: Delphine
  surname: Chinchilla
  fullname: Chinchilla, Delphine
  organization: Basel-Zurich-Plant Science Center, Botanical Institute, University Basel, Basel, Switzerland
– sequence: 11
  givenname: H Peter
  surname: van Esse
  fullname: van Esse, H Peter
  organization: Laboratory of Phytopathology, Wageningen University, Wageningen, The Netherlands
– sequence: 12
  givenname: Lucia
  surname: Jorda
  fullname: Jorda, Lucia
  organization: Centro de Biotecnología Genómica Plantas, ETSI Montes, Ciudad Universitaria s/n, Madrid, Spain
– sequence: 13
  givenname: Benjamin
  surname: Schwessinger
  fullname: Schwessinger, Benjamin
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 14
  givenname: Valerie
  surname: Nicaise
  fullname: Nicaise, Valerie
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 15
  givenname: Bart P H J
  surname: Thomma
  fullname: Thomma, Bart P H J
  organization: Laboratory of Phytopathology, Wageningen University, Wageningen, The Netherlands
– sequence: 16
  givenname: Antonio
  surname: Molina
  fullname: Molina, Antonio
  organization: Centro de Biotecnología Genómica Plantas, ETSI Montes, Ciudad Universitaria s/n, Madrid, Spain
– sequence: 17
  givenname: Jonathan D G
  surname: Jones
  fullname: Jones, Jonathan D G
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
– sequence: 18
  givenname: Cyril
  surname: Zipfel
  fullname: Zipfel, Cyril
  email: cyril.zipfel@tsl.ac.uk
  organization: The Sainsbury Laboratory, Norwich Research Park, Norwich, UK
BackLink https://www.ncbi.nlm.nih.gov/pubmed/19763086$$D View this record in MEDLINE/PubMed
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Keywords EFR
pattern‐recognition receptor
pathogen‐associated molecular patterns
SDF2
ER‐quality control
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Present address: INRA-UR 1052 Génétique et Amélioration des Fruits et Légumes, 84143 Montfavet Cedex, France
Present address: College of Plant Protection, Shangdong Agricultural University, Taian, Shandong 271018, China
These authors contributed equally to this work
Present address: Viikki Biocenter, Department of Biological and Environmental Sciences, Division of Genetics, University of Helsinki, POB 56, FIN-00014, Helsinki, Finland
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2007; 104
2000; 5
2007; 144
2002; 13
2004; 23
2008; 9
2003; 15
2008; 4
2008; 1
2003; 278
2003; 311
1997; 9
2009; 48
1998; 16
2000; 12
2005; 102
2008; 27
2005; 308
2008; 21
2008; 20
2009; 19
2006; 126
1998; 10
2007; 26
2006; 444
2006; 125
2007; 18
2004; 385
2007; 19
2007; 448
2006; 119
2000; 25
2009; 60
2008; 18
2009
2008; 56
2008; 11
2000; 275
2007; 51
2002; 417
2004; 428
1996; 15
2009; 136
1995; 8
1995; 7
2004; 16
2006; 47
2002; 21
2008; 49
2006; 48
2003; 22
2007; 49
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Snippet In plant innate immunity, the surface‐exposed leucine‐rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen‐associated...
In plant innate immunity, the surface-exposed leucine-rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen-associated...
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StartPage 3428
SubjectTerms agrobacterium-mediated transformation
Arabidopsis - immunology
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - immunology
Arabidopsis Proteins - metabolism
arabidopsis-thaliana
Botany
Carrier Proteins - metabolism
Catalysis
defective brassinosteroid receptor
disease resistance
EFR
EMBO30
EMBO31
Endoplasmic Reticulum - metabolism
endoplasmic-reticulum
ER-quality control
flagellin perception
HSP40 Heat-Shock Proteins - metabolism
Immunity, Innate
Immunology
innate immunity
Kinases
Molecular biology
pathogen-associated molecular patterns
Pathogens
pattern-recognition receptor
Physiology
Plant Diseases - immunology
pseudomonas-syringae
Quality control
Receptors, Pattern Recognition - genetics
Receptors, Pattern Recognition - immunology
Receptors, Pattern Recognition - metabolism
Retention
SDF2
secretory pathway
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Title Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity
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