The receptor MIK2 interacts with the kinase RKS1 to control quantitative disease resistance to Xanthomonas campestris

Molecular mechanisms underlying qualitative resistance have been intensively studied. In contrast, although quantitative disease resistance (QDR) is a common, durable and broad-spectrum form of immune responses in plants, only a few related functional analyses have been reported. The atypical kinase Resistance related KinaSe1 (RKS1) is a major regulator of QDR to the bacterial pathogen Xanthomonas campestris (Xcc) and is positioned in a robust protein-protein decentralized network in Arabidopsis (Arabidopsis thaliana). Among the putative interactors of RKS1 found by yeast two-hybrid screening, we identified the receptor-like kinase MDIS1-Interacting Receptor-like Kinase 2 (MIK2). Here, using multiple complementary strategies including protein-protein interaction tests, mutant analysis, and network reconstruction, we report that MIK2 is a component of RKS1­-mediated QDR to Xcc. First, by co-localization experiments, co-immunoprecipitation (Co-IP), and bimolecular fluorescence complementation (BiFC), we validated the physical interaction between RKS1 and MIK2 at the plasma membrane. Using mik2 mutants, we showed that MIK2 is required for QDR and contributes to resistance to the same level as RKS1. Interestingly, a catalytic mutant of MIK2 interacted with RKS1 but was unable to fully complement the mik2-1 mutant phenotype in response to Xcc. Finally, we investigated the potential role of the MIK2–RKS1 complex as a scaffolding component for the coordination of perception events by constructing a RKS1–MIK2 centered protein-protein interaction network. Eight mutants corresponding to seven RKs in this network showed a strong alteration in QDR to Xcc. Our findings provide insights into the molecular mechanisms underlying the perception events involved in QDR to Xcc.