Structural Basis of Teneurin-Latrophilin Interaction in Repulsive Guidance of Migrating Neurons.

ABSTRACT: Teneurins are ancient metazoan cell adhesion receptors that control brain development and neuronal wiring in higher animals. The extracellular C terminus binds the adhesion GPCR Latrophilin, forming a trans-cellular complex with synaptogenic functions. However, Teneurins, Latrophilins, and FLRT proteins are also expressed during murine cortical cell migration at earlier developmental stages. Here, we present crystal structures of Teneurin-Latrophilin complexes that reveal how the lectin and olfactomedin domains of Latrophilin bind across a spiraling beta-barrel domain of Teneurin, the YD shell. We couple structure-based protein engineering to biophysical analysis, cell migration assays, and in utero electroporation experiments to probe the importance of the interaction in cortical neuron m

SUBMITTER: Del Toro D 

PROVIDER: S-EPMC6978801 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature