Abstract
We have isolated two cDNA clones (GluR-K2 and GluR-K3) that share considerable sequence identity with the previously described glutamate receptor subunit, GluR-K1. The three glutamate receptor subunits show significant sequence conservation with the glutamine binding component of the glutamine permease of E. coli. Each of these clones encodes a channel responsive to both kainate and AMPA. The coexpression of GluR-K2 with either GluR-K3 or GluR-K1 results in the formation of channels whose current-voltage relationships differ from those of the individual subunits alone and more closely approximate the properties of kainate receptors in neurons. These observations indicate that the kainate/quisqualate receptors are encoded by a family of genes and are likely to be composed of hetero-oligomers of at least two distinct subunits.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Transport Systems, Basic*
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Animals
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Electrophysiology
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Escherichia coli / enzymology
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Escherichia coli Proteins
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Glutamates / metabolism
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Ion Channels / drug effects
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Ion Channels / physiology*
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Kainic Acid / metabolism
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Kainic Acid / pharmacology
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Membrane Proteins / genetics
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Membrane Transport Proteins / genetics
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Molecular Sequence Data
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Rats
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Rats, Inbred Strains
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Receptors, Glutamate
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Receptors, Kainic Acid
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Receptors, Neurotransmitter / chemistry
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Receptors, Neurotransmitter / genetics*
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Receptors, Neurotransmitter / physiology
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Sequence Homology, Nucleic Acid
Substances
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Amino Acid Transport Systems, Basic
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Escherichia coli Proteins
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Glutamates
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Ion Channels
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Membrane Proteins
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Membrane Transport Proteins
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Receptors, Glutamate
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Receptors, Kainic Acid
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Receptors, Neurotransmitter
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glnP protein, E coli
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glutamine permease
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Kainic Acid
Associated data
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GENBANK/X54655
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GENBANK/X54656