Extracellular salicylic acid activates immune signaling through cell-surface receptors

Salicylic acid (SA) is a central immune hormone that accumulates in both intracellular and extracellular compartments during pathogen infection. While intracellular SA signaling is well established, whether extracellular SA (eSA) directly activates immune responses remains unknown. Here we show that eSA functions as an extracellular signal potentially perceived by the plasma membrane-localized lectin receptor kinases LecRK-I.8 and LecRK-VI.2 in Arabidopsis . The extracellular domains of both receptors bind SA with micromolar affinity, SA rapidly induces LecRK-I.8 phosphorylation, and the kinase activities of LecRK-I.8 and LecRK-VI.2 are required for downstream signaling. Moreover, mutagenesis of a computationally predicted binding pocket in LecRK-VI.2 abolishes SA binding and immune function, providing evidence for receptor-mediated perception. Genetic analyses further demonstrate that LecRK receptors are required for SA-induced resistance, transcriptional reprogramming, and phosphoproteomic responses. Together, these findings expand current models of SA signaling by revealing a potential receptor-mediated cell-surface perception mechanism for a classical immune hormone.