Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses
1999 | journal article; research paper. A publication with affiliation to the University of Göttingen.
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- Authors
- Song, J. Y.; Ichtchenko, K; Südhof, Thomas C.; Brose, Nils
- Abstract
- At the synapse, presynaptic membranes specialized for vesicular traffic are linked to postsynaptic membranes specialized for signal transduction. The mechanisms that connect pre- and postsynaptic membranes into synaptic junctions are unknown. Neuroligins and beta-neurexins are neuronal cell-surface proteins that bind to each other and form asymmetric intercellular junctions, To test whether the neuroligin/beta-neurexin junction is related to synapses, we generated and characterized monoclonal antibodies to neuroligin 1. With these antibodies, we show that neuroligin 1 is synaptic. The neuronal localization, subcellular distribution, and developmental expression of neuroligin 1 are similar to those of the postsynaptic marker proteins PSD-95 and NMDA-RI receptor. Quantitative immunogold electron microscopy demonstrated that neuroligin 1 is clustered in synaptic clefts and postsynaptic densities. Double immunofluorescence labeling revealed that neuroligin I colocalizes with glutamatergic but not gamma-aminobutyric acid (GABA)ergic synapses, Thus neuroligin 1 is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors, channels, and signal-transduction molecules to synaptic sites of cell adhesion, In addition, the neuroligin/beta-neurexin junction may be involved in the specification of excitatory synapses.
- Issue Date
- 1999
- Publisher
- Natl Acad Sciences
- Journal
- Proceedings of the National Academy of Sciences
- ISSN
- 0027-8424