Tau protein is a microtubule-associated protein primarily found in neurons, where it helps stabilize microtubules, essential for maintaining the structure of neurons and facilitating intracellular transport, especially in axons. In its normal, healthy state, tau binds to and stabilizes microtubules, promoting proper neuronal function.
In pathological conditions, such as Alzheimer’s disease and other tauopathies, tau protein undergoes abnormal modifications, particularly hyperphosphorylation, which reduces its affinity for microtubules. This leads to the formation of neurofibrillary tangles (NFTs), insoluble aggregates of tau that disrupt neuronal function. The accumulation of NFTs contributes to neuronal death and neurodegeneration, affecting brain areas critical for memory, cognition, and motor function.
Tau pathology is central to several neurodegenerative disorders, including Alzheimer’s disease, frontotemporal dementia (FTD), progressive supranuclear palsy (PSP), and corticobasal degeneration (CBD). The spread of tau pathology within the brain follows a prion-like mechanism, contributing to disease progression.
Targeting tau protein aggregation and hyperphosphorylation is a major focus of research for developing therapeutic interventions in tauopathies, especially since tau pathology correlates strongly with cognitive decline in Alzheimer’s disease.
Verified by Dr. Petya Stefanova
