A two-hybrid-receptor assay demonstrates heteromer formation as switch-on for plant immune receptors

Albert, Markus and Jehle, Anna Kristina and Fürst, Ursula and Chinchilla, Delphine and Boller, Thomas and Felix, Georg. (2013) A two-hybrid-receptor assay demonstrates heteromer formation as switch-on for plant immune receptors. Plant physiology, Vol. 163, H. 4. pp. 1504-1509.

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Official URL: http://edoc.unibas.ch/dok/A6205463

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Receptor kinases sense extracellular signals and trigger intracellular signaling and physiological responses. However, how does signal binding to the extracellular domain activate the cytoplasmic kinase domain? Activation of the plant immunoreceptor Flagellin sensing2 (FLS2) by its bacterial ligand flagellin or the peptide-epitope flg22 coincides with rapid complex formation with a second receptor kinase termed brassinosteroid receptor1 associated kinase1 (BAK1). Here, we show that the receptor pair of FLS2 and BAK1 is also functional when the roles of the complex partners are reversed by swapping their cytosolic domains. This reciprocal constellation prevents interference by redundant partners that can partially substitute for BAK1 and demonstrates that formation of the heteromeric complex is the molecular switch for transmembrane signaling. A similar approach with swaps between the Elongation factor-Tu receptor and BAK1 also resulted in a functional receptor/coreceptor pair, suggesting that a "two-hybrid-receptor assay" is of more general use for studying heteromeric receptor complexes.
Faculties and Departments:05 Faculty of Science > Departement Umweltwissenschaften > Ehemalige Einheiten Umweltwissenschaften > Pflanzenphysiologie Pathogenabwehr (Boller)
UniBasel Contributors:Chinchilla, Delphine and Boller, Thomas
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:American Society of Plant Biologists
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:31 Jan 2014 09:49
Deposited On:31 Jan 2014 09:49

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