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.
LAR-RPTPs are not essential for synapse formation, but they are important determinants of synapse properties as they contribute to regulate postsynaptic NMDA receptor function.
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.
Spatial restriction of GPCR signaling at nascent synapses by adhesion complexes drives excitatory synapse formation and specificity in the hippocampus.
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.
