Structural insight into the activation of plant receptor kinases

Plant genomes encode a large family of membrane-localized receptor kinases (RKs) that play important roles in diverse biological processes by responding to a wide spectrum of external signals. RK proteins have a conserved tripartite structural organization with a divergent ectodomain (ECD), a transmembrane segment and a conserved intracellular kinase domain. Signal perception by RK-ECDs induces activation of intracellular kinase domains and consequently initiates downstream signaling. An atomic understanding of the mechanisms underlying ligand recognition by RKs and their subsequent activation would aid in engineering crop plants for agricultural practice. Recent structural studies not only reveal the basis for ligand recognition of a few RKs, but also suggest dimerization as a common way of their activation. We propose that dimerization, giving rise to apposition of two intracellular kinase domains, is a general activation mechanism of RKs.