A two-hybrid-receptor assay demonstrates heteromer formation as switch-on for plant immune receptors
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
 
ID 2280722
Author(s) Albert, Markus; Jehle, Anna Kristina; Fürst, Ursula; Chinchilla, Delphine; Boller, Thomas; Felix, Georg
Author(s) at UniBasel Chinchilla, Delphine
Boller, Thomas
Year 2013
Title A two-hybrid-receptor assay demonstrates heteromer formation as switch-on for plant immune receptors
Journal Plant physiology
Volume 163
Number 4
Pages / Article-Number 1504-9
Abstract

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.

Publisher American Society of Plant Biologists
ISSN/ISBN 0032-0889
edoc-URL http://edoc.unibas.ch/dok/A6205463
Full Text on edoc No
Digital Object Identifier DOI 10.1104/pp.113.227736
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/24130196
ISI-Number WOS:000327942800003
Document type (ISI) Journal Article
 
   

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