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

Nekrasov, V. and Li, J. and Batoux, M. and Roux, M. and Chu, Z. H. and Lacombe, S. and Rougon, A. and Bittel, P. and Kiss-Papp, M. and Chinchilla, D. and van Esse, H. P. and Jorda, L. and Schwessinger, B. and Nicaise, V. and Thomma, Bphj and Molina, A. and Jones, J. D. G. and Zipfel, C.. (2009) Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity. The EMBO journal, Vol. 28, H. 21. pp. 3428-3438.

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Official URL: http://edoc.unibas.ch/dok/A5261898

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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.
Faculties and Departments:05 Faculty of Science > Departement Umweltwissenschaften > Botanik > Pflanzenphysiologie Pathogenabwehr (Boller)
UniBasel Contributors:Chinchilla, Delphine and Bittel, Pascal and Kiss-Papp, Marta
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Nature Publishing Group
ISSN:0261-4189
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:22 Mar 2012 14:25
Deposited On:22 Mar 2012 13:46

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