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Probing the Arabidopsis flagellin receptor : FLS2-FLS2 association and the contributions of specific domains to signaling function

Sun, W. X. and Cao, Y. R. and Labby, K. J. and Bittel, P. and Boller, T. and Bent, A. F.. (2012) Probing the Arabidopsis flagellin receptor : FLS2-FLS2 association and the contributions of specific domains to signaling function. The plant cell, Vol. 24, H. 3. pp. 1096-1113.

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Official URL: http://edoc.unibas.ch/dok/A6070636

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Abstract

FLAGELLIN SENSING2 (FLS2) is a transmembrane receptor kinase that activates antimicrobial defense responses upon binding of bacterial flagellin or the flagellin-derived peptide flg22. We find that some Arabidopsis thaliana FLS2 is present in FLS2-FLS2 complexes before and after plant exposure to flg22. flg22 binding capability is not required for FLS2-FLS2 association. Cys pairs flank the extracellular leucine rich repeat (LRR) domain in FLS2 and many other LRR receptors, and we find that the Cys pair N-terminal to the FLS2 LRR is required for normal processing, stability, and function, possibly due to undescribed endoplasmic reticulum quality control mechanisms. By contrast, disruption of the membrane-proximal Cys pair does not block FLS2 function, instead increasing responsiveness to flg22, as indicated by a stronger oxidative burst. There was no evidence for intermolecular FLS2-FLS2 disulfide bridges. Truncated FLS2 containing only the intracellular domain associates with full-length FLS2 and exerts a dominant-negative effect on wild-type FLS2 function that is dependent on expression level but independent of the protein kinase capacity of the truncated protein. FLS2 is insensitive to disruption of multiple N-glycosylation sites, in contrast with the related receptor EF-Tu RECEPTOR that can be rendered nonfunctional by disruption of single glycosylation sites. These and additional findings more precisely define the molecular mechanisms of FLS2 receptor function.
Faculties and Departments:05 Faculty of Science > Departement Umweltwissenschaften > Ehemalige Einheiten Umweltwissenschaften > Pflanzenphysiologie Pathogenabwehr (Boller)
UniBasel Contributors:Boller, Thomas
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society of Plant Biologists
ISSN:1040-4651
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:01 Mar 2013 11:13
Deposited On:01 Mar 2013 11:07

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