Glyceraldehyde-3-Phosphate Dehydrogenase Is a GABAA Receptor Kinase Linking Glycolysis to Neuronal Inhibition

Protein phosphorylation is crucial for regulating synaptic transmission. We describe a novel mechanism for the phosphorylation of the GABA(A) receptor, which mediates fast inhibition in the brain. A protein copurified and coimmunoprecipitated with the phosphorylated receptor alpha1 subunit; this rec...

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Veröffentlicht in:The Journal of neuroscience 2004-09, Vol.24 (35), p.7614-7622
Hauptverfasser: Laschet, Jacques J, Minier, Frederic, Kurcewicz, Irene, Bureau, Michel H, Trottier, Suzanne, Jeanneteau, Freddy, Griffon, Nathalie, Samyn, Bart, Van Beeumen, Jozef, Louvel, Jacques, Sokoloff, Pierre, Pumain, Rene
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container_end_page 7622
container_issue 35
container_start_page 7614
container_title The Journal of neuroscience
container_volume 24
creator Laschet, Jacques J
Minier, Frederic
Kurcewicz, Irene
Bureau, Michel H
Trottier, Suzanne
Jeanneteau, Freddy
Griffon, Nathalie
Samyn, Bart
Van Beeumen, Jozef
Louvel, Jacques
Sokoloff, Pierre
Pumain, Rene
description Protein phosphorylation is crucial for regulating synaptic transmission. We describe a novel mechanism for the phosphorylation of the GABA(A) receptor, which mediates fast inhibition in the brain. A protein copurified and coimmunoprecipitated with the phosphorylated receptor alpha1 subunit; this receptor-associated protein was identified by purification and microsequencing as the key glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Molecular constructs demonstrated that GAPDH directly phosphorylates the long intracellular loop of GABA(A) receptor alpha1 subunit at identified serine and threonine residues. GAPDH and the alpha1 subunit were found to be colocalized at the neuronal plasma membrane. In keeping with the GAPDH/GABA(A) receptor molecular association, glycolytic ATP produced locally at plasma membranes was consumed for this alpha1 subunit phosphorylation, possibly within a single macrocomplex. The membrane-attached GAPDH is thus a dual-purpose enzyme, a glycolytic dehydrogenase, and a receptor-associated kinase. In acutely dissociated cortical neurons, the rundown of the GABA(A) responses was essentially attributable to a Mg(2+)-dependent phosphatase activity, which was sensitive to vanadate but insensitive to okadaic acid or fluoride. Rundown was significantly reduced by the addition of GAPDH or its reduced cofactor NADH and nearly abolished by the addition of its substrate glyceraldehyde-3-phosphate (G3P). The prevention of rundown by G3P was abolished by iodoacetamide, an inhibitor of the dehydrogenase activity of GAPDH, indicating that the GABA(A) responses are maintained by a glycolysis-dependent phosphorylation. Our results provide a molecular mechanism for the direct involvement of glycolysis in neurotransmission.
doi_str_mv 10.1523/JNEUROSCI.0868-04.2004
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source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central
subjects Adenosine Diphosphate - pharmacology
Amino Acid Sequence
Animals
Brain Chemistry
Cattle
Cell Membrane - drug effects
Cell Membrane - enzymology
Cellular/Molecular
Cercopithecus aethiops
COS Cells
Diphosphates - pharmacology
Glyceraldehyde 3-Phosphate - pharmacology
Glyceraldehyde-3-Phosphate Dehydrogenases - antagonists & inhibitors
Glyceraldehyde-3-Phosphate Dehydrogenases - isolation & purification
Glyceraldehyde-3-Phosphate Dehydrogenases - pharmacology
Glyceraldehyde-3-Phosphate Dehydrogenases - physiology
Glycolysis - physiology
Hippocampus - cytology
Iodoacetamide - pharmacology
Magnesium - pharmacology
Molecular Sequence Data
NAD - pharmacology
Neurons - drug effects
Neurons - enzymology
Phosphorylation - drug effects
Protein Interaction Mapping
Protein Processing, Post-Translational - drug effects
Protein-Serine-Threonine Kinases - antagonists & inhibitors
Protein-Serine-Threonine Kinases - isolation & purification
Protein-Serine-Threonine Kinases - physiology
Rabbits
Rats
Rats, Sprague-Dawley
Receptors, GABA-A - genetics
Receptors, GABA-A - metabolism
Recombinant Fusion Proteins - metabolism
Synaptic Transmission - drug effects
Synaptic Transmission - physiology
Transfection
title Glyceraldehyde-3-Phosphate Dehydrogenase Is a GABAA Receptor Kinase Linking Glycolysis to Neuronal Inhibition
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