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Tau aggregation is one of the major features in Alzheimer's disease and in several other tauopathies, including frontotemporal dementia with Parkinsonism linked to chromosome 17 (FTDP-17), and progressive supranuclear palsy (PSP). More than 35 mutations in the  tau  gene have been identified from FTDP-17 patients. A group of these mutations alters splicing of exon 10, resulting in an increase in exon 10 inclusion into  tau  mRNA. Abnormal splicing with inclusion of exon 10 into  tau  mRNA has also been observed in PSP and AD patients. These results indicate that abnormal splicing of exon 10, leading to the production of  tau  with exon 10, is probably one of the mechanisms by which tau accumulates and aggregates in tauopathic brains. Therefore, modulation of exon 10 splicing in the  tau  gene could potentially be targeted to prevent tauopathies. To identify small molecules or compounds that could potentially be developed into drugs to treat tauopathies, we established a cell-based high-throughput screening assay. In this review, we will discuss how realistic, specific biological molecules can be found to regulate exon 10 splicing in the  tau  gene for potential treatment of tauopathies.

Alternative splicing of exon 10 in the taugene as a target for treatment of tauopathies