Neuroligin 2 Drives Postsynaptic Assembly at Perisomatic Inhibitory Synapses through Gephyrin and Collybistin


In the mammalian CNS, each neuron typically receives thousands of synaptic inputs from diverse classes of neurons. Synaptic transmission to the postsynaptic neuron relies on localized and transmitter-specific differentiation of the plasma membrane with postsynaptic receptor, scaffolding, and adhesion proteins accumulating in precise apposition to presynaptic sites of transmitter release. We identified protein interactions of the synaptic adhesion molecule neuroligin 2 that drive postsynaptic differentiation at inhibitory synapses. Neuroligin 2 binds the scaffolding protein gephyrin through a conserved cytoplasmic motif and functions as a specific activator of collybistin, thus guiding membrane tethering of the inhibitory postsynaptic scaffold. Complexes of neuroligin 2, gephyrin and collybistin are sufficient for cell-autonomous clustering of inhibitory neurotransmitter receptors. Deletion of neuroligin 2 in mice perturbs GABAergic and glycinergic synaptic transmission and leads to a loss of postsynaptic specializations specifically at perisomatic inhibitory synapses.

DOI: 10.1016/j.neuron.2009.08.023

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@article{Poulopoulos2009Neuroligin2D, title={Neuroligin 2 Drives Postsynaptic Assembly at Perisomatic Inhibitory Synapses through Gephyrin and Collybistin}, author={Alexandros Poulopoulos and Gayane Aramuni and Guido R . Y . De Meyer and Tolga Soykan and Mrinalini Hoon and Theofilos G. Papadopoulos and Mingyue Zhang and Ingo Paarmann and C{\'e}line Fuchs and Kirsten Harvey and Peter Jedlicka and Stephan W. Schwarzacher and Heinrich Betz and Robert J Harvey and Nils Brose and Weiqi Zhang and Frederique Varoqueaux}, journal={Neuron}, year={2009}, volume={63}, pages={628-642} }