FLRT receptors act as “context identifiers” that control the formation of different signaling complexes to regulate brain development. To date, research has focused on the extracellular domain of these receptors, which allows communication between two cells.
Thanks to an international collaboration that includes French and British researchers, scientists have demonstrated a new type of interaction with the FLRT2 receptor. By combining molecular dynamics simulations with single-molecule fluorescence microscopy experiments, it was possible to quantify this interaction on the surface of the cell itself. This interaction includes both the transmembrane domain of this receptor and the extracellular domain.
This work adds an extra level of complexity to all aspects of the operation of the FLRT receiver. It provides a new basis for understanding the structural mechanisms that determine the function of these receptors in tissue growth and suggests a new mechanism for competitive binding between FLRT receptors on the same cell surface and those that can interact between two cells. · Cells.
© Mathieu Chaventthe shape: a model of the cis interaction of the FLRT2 receptor obtained by fusion Modeling of molecular dynamics (lower panel) quantifying the interaction of the transmembrane domain using small-xxx motifs and single molecule fluorescence microscopy (right panel) which allows to follow the co-diffusion of these receivers).
To learn more: The FLRT2 targeting and adhesion protein is dimerized in cis by small-X. dimer3Small membrane patterns.Jackson V, Hermann J., Tynan CJ, Rolf DJ, Corey Ra, Duncan L., Noriega M, Cho A, Kali AC, Jones EY, Sansom MSP, Martin Fernandez ML, Ciradaki E, Shavent M. structure. June 3, 2022. doi: 10.1016 / j.str.2022.05.014.