| Title | Neuroligin 2 drives postsynaptic assembly at perisomatic inhibitory synapses through gephyrin and collybistin. | | Author(s) | Poulopoulos A, Aramuni G, Meyer G, Soykan T, Hoon M, Papadopoulos T, Zhang M, Paarmann I, Fuchs C, Harvey K, Jedlicka P, Schwarzacher SW, Betz H, Harvey RJ, Brose N, Zhang W, Varoqueaux F | | Institution | Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Göttingen, Germany. | | Source | Neuron 2009 Sep 10; 63(5):628-42. | | MeSH | Animals
Brain
COS Cells
Carrier Proteins
Cell Line
Cells, Cultured
Cercopithecus aethiops
Dendrites
Glutamic Acid
Glycine
Guanine Nucleotide Exchange Factors
Humans
Membrane Proteins
Mice
Mice, Knockout
Models, Neurological
Nerve Tissue Proteins
Neurons
Rats
Receptors, GABA-A
Synapses
Synaptic Transmission
gamma-Aminobutyric Acid
| | Abstract | 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. | | Language | eng | | Pub Type(s) | In Vitro
Journal Article
Research Support, Non-U.S. Gov't
| | PubMed ID | 19755106 |
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