Thanks to an international collaboration involving French and British researchers, scientists have demonstrated a new type of FLRT2 receptor interaction. By combining molecular dynamics simulations with fluorescence microscopy experiments of a molecule, it was possible to quantify this interaction on the surface of the same cell. This interaction involves both the transmembrane region of this receptor and the extracellular domain. This task adds an extra level of complexity to all aspects of FLRT tuner operation. It provides a new basis for understanding the structural mechanisms that determine the function of these receptors in tissue growth and proposes a new competing mechanism for binding between FLRT receptors on the same cell surface and those that can interact between two cells. © Mathieu Chaventthe figure: a model of the FLRT2 receptor cis interaction obtained by modeling molecular dynamic fusion (bottom panel) quantifying transmembrane domain interaction via microscopic xxx motifs and single molecule fluorescence microscopy (right frame) of these receptors). To learn more: The FLRT2 guidance and adhesion protein is dimerized into cis via small-X. dimer3Motiva of small membranes.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.
