The guidance and adhesion protein FLRT2 dimerizes in cis via dual small-X

Autor: Verity, Jackson, Julia, Hermann, Christopher J, Tynan, Daniel J, Rolfe, Robin A, Corey, Anna L, Duncan, Maxime, Noriega, Amy, Chu, Antreas C, Kalli, E Yvonne, Jones, Mark S P, Sansom, Marisa L, Martin-Fernandez, Elena, Seiradake, Matthieu, Chavent
Rok vydání: 2021
Předmět:
Zdroj: Structure (London, England : 1993). 30(9)
ISSN: 1878-4186
Popis: Fibronectin Leucine-rich Repeat Transmembrane (FLRT 1-3) proteins are a family of broadly expressed single-spanning transmembrane receptors that play key roles in development. Their extracellular domains mediate homotypic cell-cell adhesion and heterotypic protein interactions with other receptors to regulate cell adhesion and guidance. These in trans FLRT interactions determine the formation of signaling complexes of varying complexity and function. Whether FLRTs also interact at the surface of the same cell, in cis, remains unknown. Here, molecular dynamics simulations reveal two dimerization motifs in the FLRT2 transmembrane helix. Single particle tracking experiments show that these Small-X
Databáze: OpenAIRE