Summary
Leucine‐rich repeat‐receptor‐like proteins (LRR‐RLPs) and LRR‐receptor‐like kinases (LRR‐RLKs) trigger immune signalling to promote plant resistance against pathogens. LRR‐RLPs lack an intracellular kinase domain, and several of these receptors have been shown to constitutively interact with the LRR‐RLK Suppressor of BIR1‐1/EVERSHED (SOBIR1/EVR) to form signalling‐competent receptor complexes. Ligand perception by LRR‐RLPs initiates recruitment of the co‐receptor BRI1‐Associated Kinase 1/Somatic Embryogenesis Receptor Kinase 3 (BAK1/SERK3) to the LRR‐RLP/SOBIR1 complex, thereby activating LRR‐RLP‐mediated immunity. We employed phosphorylation analysis of
in planta
‐produced proteins, live cell imaging, gene silencing and co‐immunoprecipitation to investigate the roles of SOBIR1 and BAK1 in immune signalling. We show that
Arabidopsis thaliana
(
At
) SOBIR1, which constitutively activates immune responses when overexpressed
in planta
, is highly phosphorylated
.
Moreover, in addition to the kinase activity of SOBIR1 itself, kinase‐active BAK1 is essential for
At
SOBIR1‐induced constitutive immunity and for the phosphorylation of
At
SOBIR1. Furthermore, the defence response triggered by the tomato LRR‐RLP Cf‐4 on perception of Avr4 from the extracellular pathogenic fungus
Cladosporium fulvum
is dependent on kinase‐active BAK1. We argue that, in addition to the trans‐autophosphorylation of SOBIR1, it is likely that SOBIR1 and BAK1 transphosphorylate, and thereby activate the receptor complex. The signalling‐competent cell surface receptor complex subsequently activates downstream cytoplasmic signalling partners to initiate RLP‐mediated immunity.