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- W2074369549 abstract "Slit and NTRK-like family member (Slitrk) proteins are known to have typical peptide signatures for synaptogenic cell adhesion. This study reveals a specific function of Slitrk3 and tyrosine phosphatase receptor PTPδ transynaptic interaction in inhibitory synaptogenesis and excitatory and inhibitory balance. Balanced development of excitatory and inhibitory synapses is required for normal brain function, and an imbalance in this development may underlie the pathogenesis of many neuropsychiatric disorders. Compared with the many identified trans-synaptic adhesion complexes that organize excitatory synapses, little is known about the organizers that are specific for inhibitory synapses. We found that Slit and NTRK-like family member 3 (Slitrk3) actS as a postsynaptic adhesion molecule that selectively regulates inhibitory synapse development via trans-interaction with axonal tyrosine phosphatase receptor PTPδ. When expressed in fibroblasts, Slitrk3 triggered only inhibitory presynaptic differentiation in contacting axons of co-cultured rat hippocampal neurons. Recombinant Slitrk3 preferentially localized to inhibitory postsynaptic sites. Slitrk3-deficient mice exhibited decreases in inhibitory, but not excitatory, synapse number and function in hippocampal CA1 neurons and exhibited increased seizure susceptibility and spontaneous epileptiform activity. Slitrk3 required trans-interaction with axonal PTPδ to induce inhibitory presynaptic differentiation. These results identify Slitrk3-PTPδ as an inhibitory-specific trans-synaptic organizing complex that is required for normal functional GABAergic synapse development." @default.
- W2074369549 created "2016-06-24" @default.
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- W2074369549 date "2012-01-29" @default.
- W2074369549 modified "2023-10-11" @default.
- W2074369549 title "Selective control of inhibitory synapse development by Slitrk3-PTPδ trans-synaptic interaction" @default.
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- W2074369549 doi "https://doi.org/10.1038/nn.3040" @default.
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