A-to-I editing: new and old sites, functions and speculations.
Nuclear pre-mRNA editing by selective adenosine deamination (A-to-I editing) occurs in all organisms from C. elegans to humans. This rare posttranscriptional mechanism can alter codons and hence the structure and function of proteins. New findings report new sites, give evidence that the efficiency of editing can be regulated by neurotransmitter, and reveal that an amino acid substitution introduced by editing into a neurotransmitter-gated ion channel subunit serves as a determinant for controlling the maturation, intracellular trafficking, and assembly with other subunits of this transmembrane protein.
Department of Molecular Neurobiology, Max-Planck Institute for Medical Research, Jahnstrasse 29, 69120 Heidelberg, Germany. seeburg@mpimf-heidelberg.mpg.de
Peter H
PH
Seeburg
D000241:Adenosine / Q000235:genetics / Q000378:metabolism; D000243:Adenosine Deaminase / Q000235:genetics / Q000378:metabolism; D000818:Animals; D006801:Humans; D007288:Inosine / Q000235:genetics / Q000378:metabolism; D007473:Ion Channels / Q000096:biosynthesis* / Q000235:genetics; D009420:Nervous System / Q000254:growth & development / Q000378:metabolism*; D017729:Presynaptic Terminals / Q000378:metabolism*; D017393:RNA Editing / Q000502:physiology*; D016601:RNA-Binding Proteins; D017981:Receptors, Neurotransmitter / Q000096:biosynthesis* / Q000235:genetics
D007473:Ion Channels; D016601:RNA-Binding Proteins; D017981:Receptors, Neurotransmitter; D007288:Inosine; C567955:ADARB1 protein, human; D000243:Adenosine Deaminase; D000241:Adenosine