Presynaptic adhesion molecule PTPσ in the hippocampus regulates postsynaptic NMDA receptor function and behavioral novelty recognition through mechanisms independent of their trans-synaptic binding partners.
Trans-synaptic protein interactions are required for synapse specification and function, and the combination between neuroligin3 and αneurexin1 controls inhibitory synaptic function in a splice isoform- and interneuron-specific manner.
Investigation of synapse development using a single neuron system illuminates how individual neurons specify connectivity with their postsynaptic partners and the central role of the synaptic organizer neurexin in this process.
Lasso and latrophilin-1 interact across the synapse, while shed Lasso binds latrophilin-1 on distant growth cones and attracts them, providing a universal mechanism for short- and long-range axonal guidance.
Crystal structures of synaptic recognition molecules Sidekick-1 and -2 reveal a single homodimer interaction mode responsible for both cell-cell recognition and cis-clustering, suggesting that competition between cis and trans interactions may be critical to specificity.
Neurexin–Neuroligin1 complex positively regulates F-actin assembly through direct interaction with WAVE complex to control normal synaptic growth and electrophysiological function in Drosophila neuromuscular junction.
Fly protein families Dprs and DIPs can create a multitude of complementary interfaces for homo- and heterophilic adhesion complexes, resulting in instructive roles for connectivity in the motor neuron circuitry.