GKAP-DLC2 interaction organizes the postsynaptic scaffold complex to enhance synaptic NMDA receptor activity

Journal of Cell Science
Enora MoutinJulie Perroy

Abstract

At glutamatergic brain synapses, scaffolding proteins regulate receptor location and function. The targeting and organization of scaffolding proteins in the postsynaptic density (PSD) is poorly understood, but it is known that a core protein of the glutamatergic receptor postsynaptic scaffold complex, guanylate-kinase-associated protein (GKAP) interacts with dynein light chain 2 (DLC2, also known as DYNLL2), a protein associated with molecular motors. In the present study, we combined BRET imaging, immunostaining and electrophysiological recording to assess the role of the GKAP-DLC2 interaction in the functional organization of the glutamatergic synapse. We found that GKAP-DLC2 interaction in dendritic spine stabilizes scaffolding protein expression at the PSD and enhances synaptic NMDA receptor activity. Moreover, the GKAP-DLC2 functional interaction is favored by sustained synaptic activity. These data identify a regulatory pathway of synaptic transmission that depends on activity-induced remodelling of the postsynaptic scaffold protein complex.

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Citations

May 10, 2013·The Journal of Neuroscience : the Official Journal of the Society for Neuroscience·Akira YoshiiMartha Constantine-Paton
Apr 4, 2014·International Journal of Molecular Sciences·Barbara MainoSebastiano Cavallaro
Jul 22, 2015·Journal of Ethnopharmacology·Mohammad Maqueshudul Haque BhuiyanIl Soo Moon
Jul 4, 2012·Bioarchitecture·Julie Perroy, Enora Moutin
Mar 29, 2014·BMC Neuroscience·Linda WestinHjalmar Brismar
Mar 17, 2015·PloS One·Jung-Hwa Tao-ChengAyse Dosemeci
Apr 16, 2021·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Jozef MizeraLucyna Pomierny-Chamiolo

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