Plants rely heavily on receptor-like kinases (RLKs) for perception and integration of external and internal stimuli. The Arabidopsis regulatory leucine-rich repeat RLK (LRR-RLK) BAK1 is involved in steroid hormone responses, innate immunity, and cell death control. Here, we describe the differential regulation of three different BAK1-dependent signaling pathways by a novel allele of BAK1, bak1-5. Innate immune signaling mediated by the BAK1-dependent RKs FLS2 and EFR is severely compromised in bak1-5 mutant plants. However, bak1-5 mutants are not impaired in BR signaling or cell death control. We also show that, in contrast to the RD kinase BRI1, the non-RD kinases FLS2 and EFR have very low kinase activity, and we show that neither was able to trans-phosphorylate BAK1 in vitro. Furthermore, kinase activity for all partners is completely dispensable for the ligand-induced heteromerization of FLS2 or EFR with BAK1 in planta, revealing another pathway specific mechanistic difference. The specific suppression of FLS2- and EFR-dependent signaling in bak1-5 is not due to a differential interaction of BAK1-5 with the respective ligand-binding RK but requires BAK1-5 kinase activity. Overall our results demonstrate a phosphorylation-dependent differential control of plant growth, innate immunity, and cell death by the regulatory RLK BAK1, which may reveal key differences in the molecular mechanisms underlying the regulation of ligand-binding RD and non-RD RKs.
Plants need to adapt to their ever-changing environment for survival. Transmembrane receptor kinases are essential to translate extracellular stimuli into intracellular responses. A key question is how plants maintain signaling specificity in response to multiple stresses and endogenous hormones. Growth responses induced by steroid hormones and innate immunity triggered by recognition of conserved microbial molecules depend on the common regulatory receptor-like kinase BAK1, which is also involved in cell death control. It is still unclear if BAK1 provides signaling specificity or if it is a mere signaling enhancer. Here, we describe the novel protein variant BAK1-5 that specifically blocks innate immune responses without affecting steroid responses or cell death. This unambiguously demonstrates that the role of BAK1 in plant signaling can be mechanistically separated. Importantly, the impairment of immune signaling is not caused by a loss of interaction of BAK1-5 with immune receptors but is due to an altered kinase activity. Thus, BAK1-dependent signaling pathways are under a differential phosphorylation-dependent regulation. The examination of this novel mutant version of BAK1 will enable detailed studies into the mechanistic role of BAK1 in plant innate immunity, but also more generally will provide invaluable insights into transmembrane receptor signaling specificity in plants.