Plant leucine-rich repeat receptor kinases (LRR-RKs) are able to sense small molecules as well as peptide or protein ligands. Many of those LRR-RKs rely on SERKfamily co-receptors for high affinity ligand binding and receptor association. Here, we characterize the interactions of various LRR-RKs with their cognate ligands and SERK-family co-receptors using a label-free surface biosensor based on grating-coupled interferometry (GCI).
This novel technique allows for analysis of binding partners regardless of their respective molecular weight and with high sensitivity. Due to the comparably low amount of recombinant protein and analyte needed, GCI is an excellent alternative for experiments where key components are scarce.
We demonstrate that isolated receptor LRR-ectodomains bind to their respective ligands with drastically different binding affinities, while SERK-family co-receptors bind to the ligand-associated receptors with similar kinetics. These interaction studies pinpoint the relative contributions of receptor, ligand and co-receptor to the formation and activation of active signaling units. We foresee GCI as a powerful tool to help identify novel receptor-ligand pairs as well as further co-receptors in the future.
Plant leucine-rich repeat receptor kinases (LRR-RKs) are able to sense small molecules as well as peptide or protein ligands. Many of those LRR-RKs rely on SERKfamily co-receptors for high affinity ligand binding and receptor association. Here, we characterize the interactions of various LRR-RKs with their cognate ligands and SERK-family co-receptors using a label-free surface biosensor based on grating-coupled interferometry (GCI).
This novel technique allows for analysis of binding partners regardless of their respective molecular weight and with high sensitivity. Due to the comparably low amount of recombinant protein and analyte needed, GCI is an excellent alternative for experiments where key components are scarce.
We demonstrate that isolated receptor LRR-ectodomains bind to their respective ligands with drastically different binding affinities, while SERK-family co-receptors bind to the ligand-associated receptors with similar kinetics. These interaction studies pinpoint the relative contributions of receptor, ligand and co-receptor to the formation and activation of active signaling units. We foresee GCI as a powerful tool to help identify novel receptor-ligand pairs as well as further co-receptors in the future.
