{"type":"root","children":[{"type":"paragraph","children":[{"type":"text","value":"The tau proteins are the product of alternative splicing from a single gene MAPT (microtubule-associated protein tau) located on chromosome 17. Tau are abundant in neurons of the central nervous system and are less common elsewhere, but are also expressed at very low levels in CNS astrocytes and oligodendrocytes. Tau interacts with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. It contains 85 potential serine (S), threonine (T), and tyrosine (Y) phosphorylation sites. Both the phosphorylation status and isoform expression of tau are developmentally regulated and both are important factors for cytoskeletal plasticity during embryogenesis and early development. Despite the significant heterogeneity that exists between and within the various tauopathies, the deposited tau in pathological lesions is invariably highly phosphorylated. Phosphorylation of tau at threonine 181 in particular has been linked to Alzheimer’s disease."}]}]}