title: Goldfish brain GluR2: multiple forms, RNA editing, and alternative splicing.
abstract: cDNA coding for a full-length goldfish alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) receptor subunit, GluR2, was cloned by screening unidirectional and bidirectional goldfish brain cDNA libraries. The clone has an open reading frame of 2679 bp, encoding a protein of 893 amino acids. Partial cDNA clones for three other GluR2 subunits were identified. GluR2 from goldfish brain exhibits RNA editing and alternative splicing. RNA editing occurred at the two sites demonstrated for mammalian GluR2 (Q/R and R/G). Unlike rat GluR2, GFGluR2a has a long (68 amino acids) C-terminal tail. Analysis of genomic DNA suggests that an alternatively spliced shorter C-terminal tail can be produced, similar to the rat protein. Thus, in goldfish brain, GluR2 exhibits diversity arising from multiple subtypes, RNA editing, and alternative splicing.
authors.affiliation: Department of Molecular Medicine, College of Veterinary Medicine, Cornell University, Ithaca, NY 14853, USA.
authors.forename: Z
authors.initials: Z
authors.lastname: Li
authors.forename: Z G
authors.initials: ZG
authors.lastname: Wo
authors.forename: R E
authors.initials: RE
authors.lastname: Oswald
mesh_terms: D017398:Alternative Splicing / Q000502:physiology*; D000818:Animals; D001483:Base Sequence; D001923:Brain Chemistry / Q000235:genetics*; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000032:analysis; D015870:Gene Expression / Q000502:physiology; D015723:Gene Library; D005820:Genetic Testing; D014644:Genetic Variation; D006054:Goldfish / Q000235:genetics*; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D017393:RNA Editing / Q000502:physiology*; D018091:Receptors, AMPA / Q000737:chemistry / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D013045:Species Specificity
chemical_list: D018076:DNA, Complementary; D018091:Receptors, AMPA; C104722:glutamate receptor ionotropic, AMPA 2