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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| Vydané v: | The EMBO journal Ročník 28; číslo 21; s. 3428 - 3438 |
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| Hlavní autori: | , , , , , , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | English |
| Vydavateľské údaje: |
Chichester, UK
John Wiley & Sons, Ltd
04.11.2009
Nature Publishing Group UK Springer Nature B.V Nature Publishing Group |
| Predmet: | |
| ISSN: | 0261-4189, 1460-2075, 1460-2075 |
| On-line prístup: | Získať plný text |
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| Shrnutí: | 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. |
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| Bibliografia: | ark:/67375/WNG-M9D7BQZ2-L ArticleID:EMBJ2009262 Supplementary Figures 1-17Supplementary data, Tables I-IIIReview Process istex:87FF2D11B76FA672841F122D9ABC90F8D4BBAECF ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 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 |