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58 reviewsSUMMARYPlants perceive microbe-derived molecular patterns to initiate the innate immune system. The csp22 peptide,derived from bacterial cold shock protein, is uniquely recognized by cold shock protein receptor (CORE) inSolanaceae plants, yet the signaling pathway remains largely obscure. In this study, we identify that tomatocsp22-activated kinase 1 (SlCAK1), belonging to the receptor-like cytoplasmic kinase subgroup VII, is essential for csp22-induced immune responses and resistance to bacterial wilt disease. SlCAK1 is rapidly recruitedto the csp22 receptor complex, which results in SlCAK1 phosphorylation upon csp22 treatment. Notably,csp22-induced phosphorylation specifically occurs at the Ser60 residue in the N terminus of SlCAK1, whichis critical for SlCAK1 function in immunity. Interestingly, the conservation of Ser60 is unique to Solanaceaeplants. Taken together, our findings reveal the pivotal role of SlCAK1 in transducing csp22-triggered immunesignaling and provide a novel activation mechanism for receptor-like cytoplasmic kinases that involvesphosphorylation in the N terminus.
