The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
SynCAM, a Synaptic Adhesion Molecule That Drives Synapse Assembly
Abstract
Synapses, the junctions between nerve cells through which they communicate, are formed by the coordinated assembly and tight attachment of pre- and postsynaptic specializations. We now show that SynCAM is a brain-specific, immunoglobulin domain–containing protein that binds to intracellular PDZ-domain proteins and functions as a homophilic cell adhesion molecule at the synapse. Expression of the isolated cytoplasmic tail of SynCAM in neurons inhibited synapse assembly. Conversely, expression of full-length SynCAM in nonneuronal cells induced synapse formation by cocultured hippocampal neurons with normal release properties. Glutamatergic synaptic transmission was reconstituted in these nonneuronal cells by coexpressing glutamate receptors with SynCAM, which suggests that a single type of adhesion molecule and glutamate receptor are sufficient for a functional postsynaptic response.
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Self-citationNeuroligin 1: A splice site-specific ligand for β-neurexins
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Self-citationPDZ domains in synapse assembly and signalling
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Metadata
- Authors
- Biederer, T., Sara, Y., Mozhayeva, M., Atasoy, D., Liu, X., Kavalali, E. T., & Südhof, T. C.
- Venue
- Science
- Published
- 2002-08-30
- Volume
- 297
- Issue
- 5586
- Pages
- 1525-1531
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2051434331
- Cited by
- 801
- References
- 29
- FWCI
- 13.02
- Type
- journal article
- Language
- en
- Open access
- closed
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