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Functional expression from cloned cDNAs of glutamate receptor species responsive to kainate and quisqualate
Author(s) -
Sakimura Kenji,
Bujo Hideaki,
Kushiya Etsuko,
Araki Kazuaki,
Yamazaki Makoto,
Yamazaki Masatoshi,
Meguro Hiroyuki,
Warashina Akira,
Numa Shosaku,
Mishina Masayoshi
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80452-o
Subject(s) - kainate receptor , xenopus , glutamate receptor , ampa receptor , complementary dna , biology , kainic acid , messenger rna , receptor , microbiology and biotechnology , amino acid , protein subunit , biochemistry , gene
The complete amino acid sequences of two mouse glutamate receptor subunits (GluR1 and GluR2) have been deduced by cloning and sequencing the cDNAs. Xenopus oocytes injected with mRNA derived from the GluR1 cDNA exhibit current responses both to kainate and to quisqualate as well as to glutamate, whereas oocytes injected with mRNA derived from the GluR2 cDNA show little response. Injection of oocytes with both the mRNAs produces current responses larger than those induced by the GluR1‐specific mRNA and the dose‐response relations indicate a positively cooperative interaction between the two subunits. These results suggest that kainate and quisqualate can activate a common glutamate receptor subtype and that glutamate‐gated ionic channels are hetero‐oligomers of different subunits.

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