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The microtubule-associated protein tau aggregates into insoluble filaments in numerous neurodegenerative diseases, most common of which is Alzheimer's disease. Tau aggregation in Alzheimer's disease appears to follow a continuum from soluble monomer to an end point of insoluble extracellular tangles with a strong correlation between the amount of fibrillar tau and dementia. The phosphorylation of amino acids S202 and T205 in the tau molecule is recognized by the phosphorylation-specific monoclonal antibody, AT8, and has been observed by a number of researchers to be an early step in the progression of monomer to filaments. In addition, these amino acids are located in a proline-rich region containing a set of five phosphorylation sites (one being S202), that when phosphorylated, were reported to alter several properties of tau, including filament formation. Considering these observations, we have …