Control of kinetic properties of AMPA receptor channels by nuclear RNA editing.

AMPA (alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid) receptor channels mediate the fast component of excitatory postsynaptic currents in the central nervous system. Site-selective nuclear RNA editing controls the calcium permeability of these channels, and RNA editing at a second site is shown here to affect the kinetic aspects of these channels in rat brain. In three of the four AMPA receptor subunits (GluR-B, -C, and -D), intronic elements determine a codon switch (AGA, arginine, to GGA, glycine) in the primary transcripts in a position termed the R/G site, which immediately precedes the alternatively spliced modules "flip" and "flop." The extent of editing at this site progresses with brain development in a manner specific for subunit and splice form, and edited channels possess faster recovery rates from desensitization.

[1]  H. Monyer,et al.  Glutamate-operated channels: Developmentally early and mature forms arise by alternative splicing , 1991, Neuron.

[2]  B. Sakmann,et al.  Flip and flop: a cell-specific functional switch in glutamate-operated channels of the CNS. , 1990, Science.

[3]  P. Seeburg,et al.  The organization of the gene for the functionally dominant alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor subunit GluR-B. , 1994, The Journal of biological chemistry.

[4]  J. Rossier,et al.  Subunit composition at the single-cell level explains functional properties of a glutamate-gated channel , 1994, Neuron.

[5]  Boris Barbour,et al.  Prolonged presence of glutamate during excitatory synaptic transmission to cerebellar Purkinje cells , 1994, Neuron.

[6]  M. Mayer,et al.  Cyclothiazide differentially modulates desensitization of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor splice variants. , 1994, Molecular pharmacology.

[7]  G. Wong,et al.  Molecular cloning and expression of a receptor for human tumor necrosis factor , 1990, Cell.

[8]  H. Dodt,et al.  Visualizing unstained neurons in living brain slices by infrared DIC-videomicroscopy , 1990, Brain Research.

[9]  L. Trussell,et al.  Desensitization of AMPA receptors upon multiquantal neurotransmitter release , 1993, Neuron.

[10]  P. Seeburg,et al.  RNA editing in brain controls a determinant of ion flow in glutamate-gated channels , 1991, Cell.

[11]  B. Sakmann,et al.  Differences in Ca2+ permeability of AMPA-type glutamate receptor channels in neocortical neurons caused by differential GluR-B subunit expression , 1994, Neuron.

[12]  P. Seeburg The TINS/TiPS Lecture the molecular biology of mammalian glutamate receptor channels , 1993, Trends in Neurosciences.

[13]  H. Hatt,et al.  Liquid filament switch for ultra-fast exchanges of solutions at excised patches of synaptic membrane of crayfish muscle , 1987, Neuroscience Letters.

[14]  G. Westbrook,et al.  The time course of glutamate in the synaptic cleft. , 1992, Science.

[15]  Shaul Hestrin,et al.  Activation and desensitization of glutamate-activated channels mediating fast excitatory synaptic currents in the visual cortex , 1992, Neuron.

[16]  S. Ho,et al.  Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. , 1989, Gene.

[17]  D. Melton,et al.  Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. , 1984, Nucleic acids research.

[18]  B. Sakmann,et al.  Determinants of ca2+ permeability in both TM1 and TM2 of high affinity kainate receptor channels: Diversity by RNA editing , 1993, Neuron.

[19]  J. Eberwine,et al.  Amplified RNA synthesized from limited quantities of heterogeneous cDNA. , 1990, Proceedings of the National Academy of Sciences of the United States of America.

[20]  I. Raman,et al.  Ampa receptors and rapid synaptic transmission , 1994 .

[21]  L. Trussell,et al.  Glutamate receptor desensitization and its role in synaptic transmission , 1989, Neuron.

[22]  C. Yanisch-Perron,et al.  Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. , 1985, Gene.

[23]  R. Dingledine,et al.  Identification of a site in glutamate receptor subunits that controls calcium permeability , 1991, Science.

[24]  L. Raymond,et al.  Transmembrane topology of the glutamate receptor subunit GluR6. , 1994, The Journal of biological chemistry.

[25]  J. Rossier,et al.  AMPA receptor subunits expressed by single purkinje cells , 1992, Neuron.

[26]  L. Wang,et al.  A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides. , 1994, The Journal of biological chemistry.

[27]  R. Axel,et al.  A family of glutamate receptor genes: Evidence for the formation of heteromultimeric receptors with distinct channel properties , 1990, Neuron.

[28]  P. Seeburg,et al.  RNA editing of AMPA receptor subunit GluR-B: A base-paired intron-exon structure determines position and efficiency , 1993, Cell.

[29]  S. Heinemann,et al.  Ca2+ permeability of KA-AMPA--gated glutamate receptor channels depends on subunit composition , 1991, Science.

[30]  P. Seeburg,et al.  Complex pharmacological properties of recombinant alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptor subtypes. , 1992, Molecular pharmacology.

[31]  B. Sakmann,et al.  Divalent ion permeability of AMPA receptor channels is dominated by the edited form of a single subunit , 1992, Neuron.