Inclusion of a neuroligin alternatively spliced insert that interacts with a neurexin glycan modification promote development of functional synaptic connections between neurons and may help alleviate consequences of NLGN mutations.
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.
The development of the mammalian cochlea undergoes a period of embryonic refinement in which the outer hair cell region repels incoming type I spiral ganglion neurons, thus ensuring these neurons instead form connections with inner hair cells.
Electrophysiological recordings reveal domains within the extracellular and intracellular region of neuroligin important for specifying and carrying out its function at inhibitory synapses respectively.
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.
Axonal arborisation growth is regulated by dynamic, focal localisations of Neurexin and Neuroligin that provide stability for filopodia, enabling a 'stick and grow'-based mechanism, wholly independent of synapse formation.
Neuroligin 1 is a critical adhesion molecule which organizes AMPA receptor nanodomains in close vicinity to pre-synaptic release sites, and whose genetic or chemical disruption severely impairs synaptic transmission properties.
Orthogonal to traditional paradigms that manipulate neuroligin expression level, optogenetic stimulation of tyrosine phosphorylation highlights a role of the intracellular domain of endogenous neuroligin-1 in excitatory synaptic differentiation and potentiation.