The Aggregation of Tau Protein in Alzheimer’s Disease

Currently, neurodegenerative diseases affect approximately 50 million people and are a significant cause of death and disability worldwide.One of the most well-known neurodegenerative diseases is Alzheimer's Disease.Alzheimer's Disease (AD) is characterized by the presence of neurofibrillary tangles made up of filamentous Tau aggregates and ß-amyloid depositions and is a relatively common cause of dementia in older adults.AD is known as a tauopathy, a family of neurodegenerative diseases characterized by tau neurofibrillary tangles.Neurofibrillary tangles are thought to be toxic aggregates of Tau protein that occur after tau disengages from microtubules.In neurons, microtubules are responsible for transporting substances to different parts of the cell.They exhibit dynamic instability, meaning they constantly grow and shrink.Under normal physiological conditions, Tau protein, a neuronal microtubule-associated protein, promotes microtubule self-assembly and stabilizes microtubules.Tau's intracellular interactions and functioning is regulated by phosphorylation, a post-translational modification.However, Tau undergoes hyperphosphorylation and aggregation under pathological conditions to form neurofibrillary tangles, leading to neurotoxicity.This synaptic dysfunction and loss of microtubule stability eventually lead to the neurodegeneration characteristic of tauopathies.To find new therapeutic targets, the loss of normal tau function and gain of toxic tau function must be investigated.This review will discuss the current models of Tau aggregation, the Tau pathology that causes Alzheimer's Disease, and current therapeutic strategies to treat tauopathies.