Neurexins are neuronal cell surface proteins with hundreds of isoforms generated by alternative splicing. Here we describe neuroligin 1, a neuronal cell surface protein that is enriched in synaptic plasma membranes and acts as a splice site-specific ligand for beta-neurexins. Neuroligin 1 binds to beta-neurexins only if they lack an insert in the alternatively spliced sequence of the G domain, but not if they contain an insert. The extracellular sequence of neuroligin 1 is composed of a catalytically inactive esterase domain homologous to acetylcholinesterase. In situ hybridization reveals that alternative splicing of neurexins at the site recognized by neuroligin 1 is highly regulated. These findings support a model whereby alternative splicing of neurexins creates a family of cell surface receptors that confers interactive specificity onto their resident neurons.
Pubmed ID: 7736595 RIS Download
Mesh terms: Alternative Splicing | Amino Acid Sequence | Animals | Base Sequence | Brain | Brain Chemistry | Cell Adhesion Molecules, Neuronal | Cell Membrane | Esterases | Hippocampus | Ligands | Membrane Proteins | Molecular Sequence Data | Nerve Tissue Proteins | Neurons | Protein Binding | Rats | Recombinant Proteins | Sequence Analysis | Sequence Homology, Amino Acid | Synapses | Tissue Distribution
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.