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

Vladimir Nekrasov, Jing Li, Martine Batoux, Milena Roux, Zhao Hui Chu, Severine Lacombe, Alejandra Rougon, Pascal Bittel, Marta Kiss-Papp, Delphine Chinchilla, H. Peter Van Esse, Lucia Jorda, Benjamin Schwessinger, Valerie Nicaise, Bart P.H.J. Thomma, Antonio Molina, Jonathan D.G. Jones, Cyril Zipfel*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

247 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)3428-3438
Number of pages11
JournalEMBO Journal
Volume28
Issue number21
DOIs
Publication statusPublished - Nov 2009
Externally publishedYes

Fingerprint

Dive into the research topics of 'Control of the pattern-recognition receptor EFR by an ER protein complex in plant immunity'. Together they form a unique fingerprint.

Cite this