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Tau is a microtubule-associated protein whose transcript undergoes complex regulated splicing in the mammalian nervous system. The N-terminal domain of the protein interacts with the axonal membrane, and is modulated by differential inclusion of exons 2 and 3. These two tau exons are alternatively spliced cassettes, in which exon 3 never appears independently of exon 2. Previous work with tau minigene constructs indicated that exon 3 is intrinsically suboptimal and its primary regulator is a weak branch point. In this study, we confirm the role of the weak branch point in the regulation of exon 3 but also show that the exon is additionally regulated by a combination of exonic enhancers and silencers. Furthermore, we demonstrate that known splicing regulators affect the ratio of exon 3 isoforms, Lastly, we tentatively pinpoint the site of action of several splicing factors which regulate tau exon 3.

Type

Journal article

Journal

Brain Res Mol Brain Res

Publication Date

30/05/2002

Volume

101

Pages

109 - 121

Keywords

Animals, Axons, Base Sequence, Binding Sites, COS Cells, Cell Membrane, Cell Surface Extensions, Enhancer Elements, Genetic, Exons, Gene Silencing, Genetic Vectors, Humans, Molecular Sequence Data, Mutagenesis, Site-Directed, Mutation, Nervous System, Protein Binding, Protein Isoforms, Protein Structure, Tertiary, RNA Splicing, Tumor Cells, Cultured, tau Proteins