NDLI: Up-regulation of $GABA_{B}$ Receptor Signaling by Constitutive Assembly with the $K^{+}$ Channel Tetramerization Domain-containing Protein 12 $(KCTD12)^{*}$

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Up-regulation of $GABA_{B}$ Receptor Signaling by Constitutive Assembly with the $K^{+}$ Channel Tetramerization Domain-containing Protein 12 $(KCTD12)^{*}$

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Up-regulation of $GABA_{B}$ Receptor Signaling by Constitutive Assembly with the $K^{+}$ Channel Tetramerization Domain-containing Protein 12 $(KCTD12)^{*}$

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Ivankova, Klara Seddik, Riad Fakler, Bernd Turecek, Rostislav Comps-agrar, Laëtitia Prezeau, Laurent Bettler, Bernhard Pin, Jean-philippe Fritzius, Thorsten Gassmann, Martin Besseyrias, Valerie
Description	Author Affiliation: Ivankova K ( Department of Biomedicine, University of Basel, CH-4056 Basel, Switzerland.)
Abstract	$GABA_{B}$ receptors are the G-protein coupled receptors (GPCRs) for GABA, the main inhibitory neurotransmitter in the central nervous system. Native $GABA_{B}$ receptors comprise principle and auxiliary subunits that regulate receptor properties in distinct ways. The principle subunits $GABA_{B1a},$ $GABA_{B1b},$ and $GABA_{B2}$ form fully functional heteromeric $GABA_{B(1a,2)}$ and $GABA_{B(1b,2)}$ receptors. Principal subunits regulate forward trafficking of the receptors from the endoplasmic reticulum to the plasma membrane and control receptor distribution to axons and dendrites. The auxiliary subunits KCTD8, -12, -12b, and -16 are cytosolic proteins that influence agonist potency and G-protein signaling of $GABA_{B(1a,2)}$ and $GABA_{B(1b,2)}$ receptors. Here, we used transfected cells to study assembly, surface trafficking, and internalization of $GABA_{B}$ receptors in the presence of the KCTD12 subunit. Using bimolecular fluorescence complementation and metabolic labeling, we show that $GABA_{B}$ receptors associate with KCTD12 while they reside in the endoplasmic reticulum. Glycosylation experiments support that association with KCTD12 does not influence maturation of the receptor complex. Immunoprecipitation and bioluminescence resonance energy transfer experiments demonstrate that KCTD12 remains associated with the receptor during receptor activity and receptor internalization from the cell surface. We further show that KCTD12 reduces constitutive receptor internalization and thereby increases the magnitude of receptor signaling at the cell surface. Accordingly, knock-out or knockdown of KCTD12 in cultured hippocampal neurons reduces the magnitude of the $GABA_{B}$ receptor-mediated $K^{+}$ current response. In summary, our experiments support that the up-regulation of functional $GABA_{B}$ receptors at the neuronal plasma membrane is an additional physiological role of the auxiliary subunit KCTD12.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	34
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-08-23
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hippocampus Metabolism Neurons Potassium Channels Potassium Protein Multimerization Physiology Receptors, GABA-B Signal Transduction Animals COS Cells Cell Membrane Genetics Cercopithecus Aethiops Cytology Mice Mice, Knockout Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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