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NEUROLIGIN-1 - A SPLICE SITE-SPECIFIC LIGAND FOR BETA-NEUREXINS
Author(s): ICHTCHENKO K, HATA Y, NGUYEN T, ULLRICH B, MISSLER M, MOOMAW C, SUDHOF TC
Source: CELL    Volume: 81    Issue: 3    Pages: 435-443    Published: MAY 5 1995  
Times Cited: 266     References: 25     
Abstract: 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.
Document Type: Article
Language: English
Reprint Address: ICHTCHENKO, K (reprint author), UNIV TEXAS, SW MED CTR, DEPT MOLEC GENET, DALLAS, TX 75235 USA
Addresses:
1. UNIV TEXAS, SW MED CTR, HOWARD HUGHES MED INST, DALLAS, TX 75235 USA
Publisher: CELL PRESS, 50 CHURCH ST CIRCULATION DEPT, CAMBRIDGE, MA 02138
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: QW894
ISSN: 0092-8674
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