title: Regulation of NMDA receptors in cultured hippocampal neurons by protein phosphatases 1 and 2A.
abstract: Phosphorylation of glutamate receptors is probably an important mechanism for modulating excitatory transmission. However, there is little direct evidence to indicate which protein phosphatases can dephosphorylate glutamate or other ligand-gated channels, although it is known that protein phosphatases 1 and 2A play a major part in modulating voltage and second-messenger-gated channels. Here we report that in cultured hippocampal neurons, the N-methyl-D-aspartate (NMDA) receptor can be regulated by endogenous and exogenous serine/threonine protein phosphatases. Phosphatase inhibitors enhanced NMDA currents recorded using the perforated patch technique or in cell-attached patches, whereas protein phosphatases 1 or 2A decreased the open probability of these channels in inside-out patches.
authors.affiliation: Department of Physiology, University of Toronto, Canada.
authors.forename: L Y
authors.initials: LY
authors.lastname: Wang
authors.forename: B A
authors.initials: BA
authors.lastname: Orser
authors.forename: D L
authors.initials: DL
authors.lastname: Brautigan
authors.forename: J F
authors.initials: JF
authors.lastname: MacDonald
mesh_terms: D002478:Cells, Cultured; D004988:Ethers, Cyclic / Q000494:pharmacology; D005998:Glycine / Q000378:metabolism; D006624:Hippocampus / Q000166:cytology / Q000378:metabolism*; D008387:Marine Toxins; D008564:Membrane Potentials; D016202:N-Methylaspartate / Q000378:metabolism; D009474:Neurons / Q000378:metabolism*; D019319:Okadaic Acid; D010080:Oxazoles / Q000494:pharmacology; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D016194:Receptors, N-Methyl-D-Aspartate / Q000378:metabolism*
chemical_list: D004988:Ethers, Cyclic; D008387:Marine Toxins; D010080:Oxazoles; D016194:Receptors, N-Methyl-D-Aspartate; D019319:Okadaic Acid; D016202:N-Methylaspartate; C059041:calyculin A; D010749:Phosphoprotein Phosphatases; D005998:Glycine