title: Somatodendritic localization of Translin, a component of the Translin/Trax RNA binding complex.
abstract: Recent studies implicating dendritic protein synthesis in synaptic plasticity have focused attention on identifying components of the molecular machinery involved in processing dendritic RNA. Although Translin was originally identified as a protein capable of binding single-stranded DNA, subsequent studies have demonstrated that it also binds RNA in vitro. Because previous studies indicated that Translin-containing RNA/single-stranded DNA binding complexes are highly enriched in brain, we and others have proposed that it may be involved in dendritic RNA processing. To assess this possibility, we have conducted studies aimed at defining the localization of Translin and its partner protein, Trax, in brain. In situ hybridization studies demonstrated that both Translin and Trax are expressed in neurons with prominent staining apparent in cerebellar Purkinje cells and neuronal layers of the hippocampus. Subcellular fractionation studies demonstrated that both Translin and Trax are highly enriched in the cytoplasmic fraction compared with nuclear extracts. Furthermore, immunohistochemical studies with Translin antibodies revealed prominent staining in Purkinje neuron cell bodies that extends into proximal and distal dendrites. A similar pattern of somatodendritic localization was observed in hippocampal and neocortical pyramidal neurons. These findings demonstrate that Translin is expressed in neuronal dendrites and therefore support the hypothesis that the Translin/Trax complex may be involved in dendritic RNA processing.
authors.affiliation: Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
authors.forename: P M
authors.initials: PM
authors.lastname: Finkenstadt
authors.forename: W S
authors.initials: WS
authors.lastname: Kang
authors.forename: M
authors.initials: M
authors.lastname: Jeon
authors.forename: E
authors.initials: E
authors.lastname: Taira
authors.forename: W
authors.initials: W
authors.lastname: Tang
authors.forename: J M
authors.initials: JM
authors.lastname: Baraban
mesh_terms: D000818:Animals; D001667:Binding, Competitive; D001921:Brain / Q000166:cytology / Q000378:metabolism; D001923:Brain Chemistry; D002352:Carrier Proteins / Q000032:analysis* / Q000378:metabolism; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000737:chemistry; D003593:Cytoplasm / Q000737:chemistry; D004268:DNA-Binding Proteins / Q000032:analysis* / Q000378:metabolism; D003712:Dendrites / Q000378:metabolism*; D007150:Immunohistochemistry; D046911:Macromolecular Substances; D008297:Male; D009474:Neurons / Q000737:chemistry* / Q000166:cytology / Q000378:metabolism; D009687:Nuclear Proteins / Q000032:analysis* / Q000378:metabolism; D011233:Precipitin Tests; D012313:RNA / Q000378:metabolism; D016601:RNA-Binding Proteins / Q000032:analysis / Q000378:metabolism; D051381:Rats; D013347:Subcellular Fractions / Q000737:chemistry
chemical_list: D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D009687:Nuclear Proteins; D016601:RNA-Binding Proteins; C498304:Tsn protein, rat; C498307:Tsnax protein, rat; D012313:RNA