The tomato brassinosteroid receptor BRI1 increases binding of systemin to tobacco plasma membranes, but is not involved in systemin signaling

UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Publication Date


Document Type



Amino Acid Sequence; Brassinosteroids; Cell Membrane; Cells, Cultured; Cholestanols; Fluorescent Dyes; Gene Silencing; Immunoblotting; Immunoprecipitation; Lycopersicon esculentum; Microscopy, Fluorescence; Molecular Sequence Data; Peptides; Phosphorylation; Plant Proteins; Plants, Genetically Modified; Protein Binding; Protein Kinases; Reverse Transcriptase Polymerase Chain Reaction; *Signal Transduction; Steroids, Heterocyclic; Threonine; Tobacco


Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Plant Biology | Therapeutics


The tomato wound signal systemin is perceived by a specific high-affinity, saturable, and reversible cell surface receptor. This receptor was identified as the receptor-like kinase SR160, which turned out to be identical to the brassinosteroid receptor BRI1. Recently, it has been shown that the tomato bri1 null mutant cu3 is as sensitive to systemin as wild type plants. Here we explored these contradictory findings by studying the responses of tobacco plants (Nicotiana tabacum) to systemin. A fluorescently-labeled systemin analog bound specifically to plasma membranes of tobacco suspension-cultured cells that expressed the tomato BRI1-FLAG transgene, but not to wild type tobacco cells. On the other hand, signaling responses to systemin, such as activation of mitogen-activated protein kinases and medium alkalinization, were neither increased in BRI1-FLAG-overexpressing tobacco cells nor decreased in BRI1-silenced cells as compared to levels in untransformed control cells. Furthermore, in transgenic tobacco plants BRI1-FLAG became phosphorylated on threonine residues in response to brassinolide application, but not in response to systemin. When BRI1 transcript levels were reduced by virus-induced gene silencing in tomato plants, the silenced plants displayed a phenotype characteristic of bri1 mutants. However, their response to overexpression of the Prosystemin transgene was the same as in control plants. Taken together, our data suggest that BRI1 can function as a systemin binding protein, but that binding of the ligand does not transduce the signal into the cell. This unusual behavior and the nature of the elusive systemin receptor will be discussed.


Systemin, SR160, BRI1, Wound response, Wound signaling, Brassinosteroids

DOI of Published Version



Plant Mol Biol. 2009 Jul;70(5):603-16. doi: 10.1007/s11103-009-9494-x. Link to article on publisher's site. Epub 2009 Apr 29.

Journal/Book/Conference Title

Plant molecular biology


At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

Related Resources

Link to Article in PubMed