Abstract
In recent years, secreted peptides have been recognized as essential mediators of intercellular communication which governs plant growth, development, environmental interactions, and other mediated biological responses, such as stem cell homeostasis, cell proliferation, wound healing, hormone sensation, immune defense, and symbiosis, among others. Many of the known secreted peptide ligand receptors belong to the leucine-rich repeat receptor kinase (LRR-RK) family of membrane integral receptors, which contain more than 200 members within Arabidopsis making it the largest family of plant receptor kinases (RKs). Genetic and biochemical studies have provided valuable data regarding peptide ligands and LRR-RKs, however, visualization of ligand/LRR-RK complex structures at the atomic level is vital to understand the functions of LRR-RKs and their mediated biological processes. The structures of many plant LRR-RK receptors in complex with corresponding ligands have been solved by X-ray crystallography, revealing new mechanisms of ligand-induced receptor kinase activation. In this review, we briefly elaborate the peptide ligands, and aim to detail the structures and mechanisms of LRR-RK activation as induced by secreted peptide ligands within plants.
Highlights
Plant development is mostly a post-embryonic event in which intercellular signaling and cell-cell communication play a large role [1]
This review aims to highlight the structural characterization of multiple leucine-rich repeat receptor kinase (LRR-receptor kinases (RKs)) ectodomains and their complexes with corresponding peptide ligands and co-receptors that have broadened our knowledge about plant receptor kinase activation
LRR containing proteins have been identified in archaea, bacteria, eukaryotes and even in viruses [171]
Summary
Plant development is mostly a post-embryonic event in which intercellular signaling and cell-cell communication play a large role [1]. Membrane integral receptor kinases (RKs) are necessary for the plant intercellular signaling network as they perceive these secreted peptides and allow plants to respond to various external and internal cues to regulate their growth and development. This review aims to highlight the structural characterization of multiple LRR-RK ectodomains and their complexes with corresponding peptide ligands and co-receptors that have broadened our knowledge about plant receptor kinase activation. In Arabidopsis thaliana, studies predict that more than 1000 genes may encode secreted peptides [72] These findings suggest that similar to other eukaryotes, plants employ peptide hormones as intercellular signaling molecules. Within plants, secreted peptides act extracellularly and are recognized by the transmembrane receptors present on the neighboring cells and can regulate cellular signaling pathways. We will focus mainly on the peptide ligands and their corresponding LRR-RLKs that have been structurally characterized
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