Shisa6 traps AMPA receptors at postsynaptic sites and prevents their desensitization during synaptic activity

Remco V. Klaassen, Jasper Stroeder, Françoise Coussen, Anne-Sophie Hafner, Jennifer D. Petersen, Cedric Renancio, Leanne J. M. Schmitz, Elisabeth Normand, Johannes C. Lodder, Diana C. Rotaru, Priyanka Rao-Ruiz, Sabine Spijker, Huibert D. Mansvelder, Daniel Choquet and August B. Smit ()
Additional contact information
Remco V. Klaassen: Department Molecular and Cellular Neurobiology
Jasper Stroeder: Department Molecular and Cellular Neurobiology
Françoise Coussen: University of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297
Anne-Sophie Hafner: University of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297
Jennifer D. Petersen: University of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297
Cedric Renancio: University of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297
Leanne J. M. Schmitz: Department Molecular and Cellular Neurobiology
Elisabeth Normand: University of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297
Johannes C. Lodder: Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University
Diana C. Rotaru: Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University
Priyanka Rao-Ruiz: Department Molecular and Cellular Neurobiology
Sabine Spijker: Department Molecular and Cellular Neurobiology
Huibert D. Mansvelder: Center for Neurogenomics and Cognitive Research, Neuroscience Campus Amsterdam, VU University
Daniel Choquet: University of Bordeaux, Interdisciplinary Institute for Neuroscience, UMR 5297
August B. Smit: Department Molecular and Cellular Neurobiology

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: Abstract Trafficking and biophysical properties of AMPA receptors (AMPARs) in the brain depend on interactions with associated proteins. We identify Shisa6, a single transmembrane protein, as a stable and directly interacting bona fide AMPAR auxiliary subunit. Shisa6 is enriched at hippocampal postsynaptic membranes and co-localizes with AMPARs. The Shisa6 C-terminus harbours a PDZ domain ligand that binds to PSD-95, constraining mobility of AMPARs in the plasma membrane and confining them to postsynaptic densities. Shisa6 expressed in HEK293 cells alters GluA1- and GluA2-mediated currents by prolonging decay times and decreasing the extent of AMPAR desensitization, while slowing the rate of recovery from desensitization. Using gene deletion, we show that Shisa6 increases rise and decay times of hippocampal CA1 miniature excitatory postsynaptic currents (mEPSCs). Shisa6-containing AMPARs show prominent sustained currents, indicating protection from full desensitization. Accordingly, Shisa6 prevents synaptically trapped AMPARs from depression at high-frequency synaptic transmission.

Date: 2016
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DOI: 10.1038/ncomms10682

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