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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Published in:The EMBO journal Vol. 28; no. 21; pp. 3428 - 3438
Main Authors: 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
Format: Journal Article
Language:English
Published: Chichester, UK John Wiley & Sons, Ltd 04.11.2009
Nature Publishing Group UK
Springer Nature B.V
Nature Publishing Group
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ISSN:0261-4189, 1460-2075, 1460-2075
Online Access:Get full text
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Summary: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.
Bibliography:ark:/67375/WNG-M9D7BQZ2-L
ArticleID:EMBJ2009262
Supplementary Figures 1-17Supplementary data, Tables I-IIIReview Process
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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
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1038/emboj.2009.262