Literature DB >> 1717158

RNA editing in brain controls a determinant of ion flow in glutamate-gated channels.

B Sommer1, M Köhler, R Sprengel, P H Seeburg.   

Abstract

L-glutamate, the principal excitatory transmitter in the brain, gates ion channels mediating fast neurotransmission. Subunit components of two related classes of glutamate receptor channels have been characterized by cDNA cloning and shown to carry either an arginine or a glutamine residue in a defined position of their putative channel-forming segment. The arginine residue in this segment profoundly alters, and dominates, the properties of ion flow, as demonstrated for one channel class. We now show that the genomic DNA sequences encoding the particular channel segment of all subunits harbor a glutamine codon (CAG), even though an arginine codon (CGG) is found in mRNAs of three subunits. Multiple genes and alternative exons were excluded as sources for the arginine codon; hence, we propose that transcripts for three subunits are altered by RNA editing. This process apparently edits subunit transcripts of the two glutamate receptor classes with different efficiency and selectivity.

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Year:  1991        PMID: 1717158     DOI: 10.1016/0092-8674(91)90568-j

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  440 in total

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2.  The solution structure of the Zalpha domain of the human RNA editing enzyme ADAR1 reveals a prepositioned binding surface for Z-DNA.

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4.  Correlation of AMPA receptor subunit composition with synaptic input in the mammalian cochlear nuclei.

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Review 5.  RNA editing by adenosine deaminases that act on RNA.

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6.  Elevated activity of the large form of ADAR1 in vivo: very efficient RNA editing occurs in the cytoplasm.

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7.  Coordination of editing and splicing of glutamate receptor pre-mRNA.

Authors:  Eva Bratt; Marie Ohman
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8.  A novel allosteric potentiator of AMPA receptors: 4--2-(phenylsulfonylamino)ethylthio--2,6-difluoro-phenoxyaceta mide.

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9.  A third member of the RNA-specific adenosine deaminase gene family, ADAR3, contains both single- and double-stranded RNA binding domains.

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Journal:  RNA       Date:  2000-05       Impact factor: 4.942

10.  Differing intrinsic biological properties between forebrain and spinal oligodendroglial lineage cells.

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