Abstract
Brassinosteroids (BRs) are a class of growth-promoting steroid hormones in plants, which are sensed by the membrane receptor kinase BRASSINOSTEROID INSENSITIVE 1 (BRI1). BR binding to the extracellular domain of BRI1 creates a docking platform for shape-complementary co-receptor kinases of the SOMATIC EMBRYOGENESIS RECEPTOR-LIKE KINASE (SERK) family. Ligand-induced hetero-dimerization of BRI1 with a SERK co-receptor at the cell surface renders their cytoplasmic kinase domains competent to trans-phosphorylate and activate each other. The fully active BRI1 kinase domain can then initiate a cytoplasmic signaling cascade, leading to substantial changes in gene expression. Here, we summarize our current mechanistic understanding of brassinosteroid sensing and BRI1 receptor activation.
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