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Nicotinamide adenine dinucleotide (NAD + ) participates in intracellular and extracellular signaling events unrelated to metabolism. In animals, purinergic receptors are required for extracellular NAD +  (eNAD + ) to evoke biological responses, indicating that eNAD +  may be sensed by cell-surface receptors. However, the identity of eNAD + -binding receptors still remains elusive. Here, we identify a lectin receptor kinase (LecRK), LecRK-I.8, as a potential eNAD +  receptor in  Arabidopsis . The extracellular lectin domain of LecRK-I.8 binds NAD +  with a dissociation constant of 436.5 ± 104.8 nM, although much higher concentrations are needed to trigger in vivo responses. Mutations in  LecRK-I.8  inhibit NAD + -induced immune responses, whereas overexpression of  LecRK-I.8  enhances the  Arabidopsis  response to NAD + . Furthermore,  LecRK-I.8  is required for basal resistance against bacterial pathogens, substantiating a role for eNAD +  in plant immunity. Our results demonstrate that lectin receptors can potentially function as eNAD + -binding receptors and provide direct evidence for eNAD +  being an endogenous signaling molecule in plants.

A lectin receptor kinase as a potential sensor for extracellular nicotinamide adenine dinucleotide in Arabidopsis thaliana