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Science 30 August 2002:
Vol. 297. no. 5586, pp. 1525 - 1531
DOI: 10.1126/science.1072356

Research Articles

SynCAM, a Synaptic Adhesion Molecule That Drives Synapse Assembly

Thomas Biederer,1* Yildirim Sara,1 Marina Mozhayeva,1 Deniz Atasoy,1 Xinran Liu,12 Ege T. Kavalali,13 Thomas C. Südhof124*

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.

1 Center for Basic Neuroscience, Departments of
2 Molecular Genetics, and
3 Physiology, and
4 Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.
*   To whom correspondence should be addressed. E-mail: Thomas.Sudhof{at}UTSouthwestern.edu (T.C.S.); Thomas.Biederer{at}UTSouthwestern.edu (T.B.)


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