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The Journal of Neuroscience, August 16, 2006, 26(33):8502-8511; doi:10.1523/JNEUROSCI.1758-06.2006

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Cellular/Molecular
Cytoskeleton Regulation of Glycine Receptor Number at Synapses and Diffusion in the Plasma Membrane

Cécile Charrier,¹ Marie-Virginie Ehrensperger,² Maxime Dahan,² Sabine Lévi,¹ and Antoine Triller¹

¹Laboratoire de Biologie Cellulaire de la Synapse, Institut National de la Santé et de la Recherche Médicale, Unité 789, Ecole Normale Supérieure, 75005 Paris, France, and ²Laboratoire Kastler Brossel, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 8552, Ecole Normale Supérieure and Université Pierre et Marie Curie, 75005 Paris, France

Correspondence should be addressed to Antoine Triller, Laboratoire de Biologie Cellulaire de la Synapse, Institut National de la Santé et de la Recherche Médicale Unité 789, Ecole Normale Supérieure, 46 rue d’Ulm, 75005 Paris, France. Email: triller{at}biologie.ens.fr

Lateral diffusion of neurotransmitter receptors in and out of synapses has been postulated as a core mechanism for rapid changes in receptor number at synapses during plastic processes. In this study, we have used single particle tracking to investigate how changes in glycine receptor (GlyR) lateral diffusion properties might account for changes in receptor number at synapses after disruption of the cytoskeleton in dissociated spinal cord neurons. We found that pharmacological disruption of F-actin and microtubules decreased the amount of GlyR and gephyrin, the backbone of the inhibitory postsynaptic scaffold, at synapses. F-actin and microtubule disruption increased GlyR exchanges between the synaptic and extrasynaptic membranes and decreased receptor dwell time at synapses. GlyR lateral diffusion was predominantly controlled by microtubules in the extrasynaptic membrane and by actin at synapses. Both diffusion coefficients and confinement at synapses were affected after F-actin disruption. Our results indicate that receptor exchanges between the synaptic and extrasynaptic compartments depend on the properties of both the postsynaptic differentiation and the extrasynaptic membrane. Consequently, GlyR number at synapses may be rapidly modulated by the cytoskeleton through the regulation of lateral diffusion in the plasma membrane and of receptor stabilization at synapses.

Key words: inhibitory synapses; glycine receptor; lateral diffusion; single particle tracking; cytoskeleton; plasma membrane

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Received April 25, 2006; revised June 14, 2006; accepted June 15, 2006.

Correspondence should be addressed to Antoine Triller, Laboratoire de Biologie Cellulaire de la Synapse, Institut National de la Santé et de la Recherche Médicale Unité 789, Ecole Normale Supérieure, 46 rue d’Ulm, 75005 Paris, France. Email: triller{at}biologie.ens.fr

This article has been cited by other articles:

				M. Calamai, C. G. Specht, J. Heller, D. Alcor, P. Machado, C. Vannier, and A. Triller Gephyrin Oligomerization Controls GlyR Mobility and Synaptic Clustering J. Neurosci., June 17, 2009; 29(24): 7639 - 7648. [Abstract] [Full Text] [PDF]

				M. Renner, D. Choquet, and A. Triller Control of the Postsynaptic Membrane Viscosity J. Neurosci., March 4, 2009; 29(9): 2926 - 2937. [Abstract] [Full Text] [PDF]

				E. G. Bruneau, J. A. Esteban, and M. Akaaboune Receptor-associated proteins and synaptic plasticity FASEB J, March 1, 2009; 23(3): 679 - 688. [Abstract] [Full Text] [PDF]

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				A. M. Pooler and R. A. J. McIlhinney Lateral Diffusion of the GABAB Receptor Is Regulated by the GABAB2 C Terminus J. Biol. Chem., August 31, 2007; 282(35): 25349 - 25356. [Abstract] [Full Text] [PDF]

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