Abstract
The carboxyl-terminal domain of the zeta 1 subunit of the mouse NMDA receptor channel produced as a fusion protein with GST was phosphorylated in vitro by PKC. A mutant of the zeta 1 subunit without serine or threonine residues in the carboxyl-terminal domain (zeta 1-2-NST) was constructed and was expressed alone or together with the epsilon 2 subunit in Xenopus oocytes. Current responses of the zeta 1-2-NST homomeric and epsilon 2/zeta 1-2-NST heteromeric NMDA receptor channels were enhanced by treatment with TPA, a PKC activator, and the extents of potentiation were comparable with the corresponding wild-type channels. These results suggest that the phosphorylation of the carboxyl-terminal domain of the zeta 1 subunit is not responsible for potentiation of NMDA receptor channels by the TPA treatment.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Electrophoresis, Polyacrylamide Gel
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Ion Channels / biosynthesis
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Ion Channels / drug effects
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Ion Channels / physiology*
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Macromolecular Substances
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Mice
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oocytes / drug effects
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Oocytes / physiology
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Peptide Fragments / metabolism
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Phosphorylation
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Polymerase Chain Reaction
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Protein Kinase C / metabolism
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RNA, Messenger / metabolism
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Receptors, N-Methyl-D-Aspartate / biosynthesis
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Receptors, N-Methyl-D-Aspartate / drug effects
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Receptors, N-Methyl-D-Aspartate / physiology*
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Recombinant Fusion Proteins / drug effects
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Recombinant Fusion Proteins / isolation & purification
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Recombinant Fusion Proteins / metabolism
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Tetradecanoylphorbol Acetate / pharmacology*
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Xenopus
Substances
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Ion Channels
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Macromolecular Substances
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Peptide Fragments
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RNA, Messenger
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Receptors, N-Methyl-D-Aspartate
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Recombinant Fusion Proteins
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Protein Kinase C
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Tetradecanoylphorbol Acetate