In the GluR1 glutamate receptor subunit a glutamine to histidine point mutation suppresses inward rectification but not calcium permeability.

Article date: 1992/2/14

PubMed ID: 1371672

Journal name: Biochemical and biophysical research communications (ISSN: 0006-291X)


Recent papers have described glutamine to arginine point mutations of the cloned AMPA/Kainate receptor subunits that alter current-voltage relationship and suppress Ca2+ permeability, thus linking these two characteristics. We describe a glutamine to histidine mutation at the same position, which alters current-voltage relationship but retains Ca2+ permeability, thus dissociating the two properties.

Author List: Curutchet P, Bochet P, Prado de Carvalho L, Lambolez B, Stinnakre J, Rossier J

Publication Types: Journal Article

Substances mentioned in the article: Calcium Channels; Glutamates; Macromolecular Substances; Oligodeoxyribonucleotides; Quinoxalines; Receptors, Glutamate; Receptors, Neurotransmitter; Glutamine; Barium; Ibotenic Acid; Histidine; FG 9041; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid; Kainic Acid; Calcium;

Mesh terms: Animals; Barium/pharmacology; Base Sequence; Calcium/metabolism; Calcium Channels/drug effects; Cloning, Molecular; Evoked Potentials/drug effects; Glutamates/metabolism; Glutamine; Histidine; Ibotenic Acid/analogs & derivatives; Kainic Acid/pharmacology; Macromolecular Substances; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Oocytes/drug effects; Plasmids; Quinoxalines/pharmacology; Receptors, Glutamate; Receptors, Neurotransmitter/genetics; Transcription, Genetic; Xenopus laevis; alpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid;

1371672.txt ยท Last modified: 2018/11/20 14:26 (external edit)