Interacting partners of Tau protein in Alzheimer's disease

Alzheimer's disease (AD) is an irreversible neurodegenerative condition causes noticeable symptoms including impaired memory and cognitive decline. In AD, the intracellular aggregation of Tau into NFTs is the histopathological indicator that impairs the neuronal function. Tau is a highly soluble, intrinsically disordered in nature, allowing it to adopt multiple conformation. Tau, a microtubule-associated protein, it interacts with tubulin subunits and plays a critical role in stabilizing microtubule network. Tau protein interacts with numerous proteins in physiological and pathological conditions. This interaction facilitating either biological function or contribute to Tau-mediated pathogenic changes. Tau interacting partners and related molecular crossroads can either propagate Tau pathogenesis, or they have neuroprotective role, lowering toxic Tau species or inflammation. In the central nervous system, Tau function is regulated by posttranslational modification at many sites within the protein. Tau in functioning neurons contains numerous phosphate groups, the majority of which are found in the microtubule assembly domain. Hyperphosphorylation and aggregation of Tau are the significant pathological markers of AD. This review focuses on Tau as a multifunctional protein and its known interaction partners involved in the control of several processes.