Neuroligin-4 is localized to glycinergic postsynapses and regulates inhibition in the retina
| Autor: | Siegrid Löwel, Tolga Soykan, Björn H. Falkenburger, Annarita Patrizi, Nils Brose, Frederique Varoqueaux, Tobias Moser, Marco Sassoè-Pognetto, Mrinalini Hoon, Holger Taschenberger, Matthieu Hammer, Karl-Friedrich Schmidt |
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| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Central Nervous System
Patch-Clamp Techniques viruses Cell Adhesion Molecules Neuronal Blotting Western Synaptogenesis Neuroligin Inhibitory postsynaptic potential Postsynapse Retina 03 medical and health sciences Mice 0302 clinical medicine Receptors Glycine Postsynaptic potential immune system diseases Two-Hybrid System Techniques Chlorocebus aethiops Electroretinography Animals Immunoprecipitation Glycine receptor 030304 developmental biology 0303 health sciences Multidisciplinary Microscopy Confocal biology Gephyrin virus diseases Antibodies Monoclonal Membrane Proteins Neural Inhibition biochemical phenomena metabolism and nutrition Biological Sciences Immunohistochemistry Immunology COS Cells Synapses biology.protein Electrophoresis Polyacrylamide Gel Carrier Proteins Collybistin Neuroscience 030217 neurology & neurosurgery |
| Zdroj: | Proceedings of the National Academy of Sciences; Vol 108 Proceedings of the National Academy of Sciences Proceedings of the National Academy of Sciences of the United States of America |
| ISSN: | 1091-6490 |
| DOI: | 10.1073/pnas.1006946108 |
| Popis: | Neuroligins (NL1–NL4) are postsynaptic adhesion proteins that control the maturation and function of synapses in the central nervous system (CNS). Loss-of-function mutations in NL4 are linked to rare forms of monogenic heritable autism, but its localization and function are unknown. Using the retina as a model system, we show that NL4 is preferentially localized to glycinergic postsynapses and that the loss of NL4 is accompanied by a reduced number of glycine receptors mediating fast glycinergic transmission. Accordingly, NL4-deficient ganglion cells exhibit slower glycinergic miniature postsynaptic currents and subtle alterations in their stimulus-coding efficacy, and inhibition within the NL4-deficient retinal network is altered as assessed by electroretinogram recordings. These data indicate that NL4 shapes network activity and information processing in the retina by modulating glycinergic inhibition. Importantly, NL4 is also targeted to inhibitory synapses in other areas of the CNS, such as the thalamus, colliculi, brainstem, and spinal cord, and forms complexes with the inhibitory postsynapse proteins gephyrin and collybistin in vivo, indicating that NL4 is an important component of glycinergic postsynapses. |
| Databáze: | OpenAIRE |
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