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It has also been proposed that tau interacts with components of the neural plasma membrane through its N-terminal domain, presumably via an interaction with the membrane-binding protein annexin A2 .In addition, tau isoforms in possession of different numbers of N-terminal inserts display distinct protein interaction patterns.
The microtubule binding domain consists of four imperfectly repeated motifs, separated by flanking regions, which together provide the primary structures by which tau binds and stabilises microtubules.
Finally, we describe the cascade of pathological events that may be driven by tau dysfunction, including impaired axonal transport, alterations in synapse and mitochondrial function, activation of the unfolded protein response and defective protein degradation.
It is important to fully understand the range of neuronal functions attributed to tau, since this will provide vital information on its involvement in the development and pathogenesis of disease.
Tau is well established as a microtubule-associated protein in neurons.
However, under pathological conditions, aberrant assembly of tau into insoluble aggregates is accompanied by synaptic dysfunction and neural cell death in a range of neurodegenerative disorders, collectively referred to as tauopathies.