Abstract
GluR1 and GluR2 are two highly homologous subunits of the glutamate AMPA receptor but with different functional properties. In ligand gated channels the transmembrane domain II is thought to form the wall of the ionic pore and determine the electrical properties. A chimeric AMPA receptor subunit was constructed by replacing the region comprising transmembrane domains I and II in GluR1 by the corresponding region of GluR2. Alone or forming an heteromer with GluR1, the resulting chimera has the properties of GluR2. Sequence comparison suggests that an arginine at position 600 in the chimera instead of a glutamine in GluR1 is responsible for these properties.
Publication types
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Comparative Study
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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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Base Sequence
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Chimera*
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Gene Expression
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Ion Channels / drug effects
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Ion Channels / physiology*
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Kainic Acid / pharmacology*
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Macromolecular Substances
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Membrane Potentials / drug effects
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Molecular Sequence Data
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Oligonucleotide Probes
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Oocytes / drug effects
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Oocytes / physiology
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Protein Conformation
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Quisqualic Acid / pharmacology*
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RNA Splicing
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Receptors, AMPA
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Receptors, Glutamate
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Receptors, Neurotransmitter / drug effects
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Receptors, Neurotransmitter / genetics
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Receptors, Neurotransmitter / physiology*
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Sequence Homology, Nucleic Acid
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Transcription, Genetic
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Xenopus laevis
Substances
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Ion Channels
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Macromolecular Substances
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Oligonucleotide Probes
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Receptors, AMPA
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Receptors, Glutamate
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Receptors, Neurotransmitter
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Quisqualic Acid
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Kainic Acid