The Structure of Tau Proteins and Its Role in Neurodegenerative Disease

Abstract

Abundant in the nerve cells of the central nervous system, tau proteins primarily serve to help maintain the stabilization of microtubules in axons (Michalicova et al., 2020). These microtubules are essential for the rigid structure of the cell and allow for intracellular transport of nutrients and other molecules (Parker et al., 2014). Tau proteins, using polymerization, regulate microtubule stability by binding between the tubulin heterodimers, which form the microtubules. Irregular interaction between tau proteins and microtubules can lead to associated neurodegenerative diseases called tauopathies. While there are many tauopathies, such as frontotemporal dementia with parkinsonism‐17 and Pick disease, Alzheimer’s is one of the most prevalent and studied diseases associated with tau (Gao et al., 2018). Tau protein aggression causes neurofibrillary tangles that deteriorate the microtubules’ structure, thus eventually blocking the synaptic communication between neurons (NIH National Institute on Aging, 2017). Over the past few years, numerous research has been conducted for potential tau immunotherapies, raising hopes for a possible solution (Congdon & Sigurdsson, 2018). Microtubule‐stabilizing drugs may also be instrumental in easing neurodegenerative diseases (Kadavath et al., 2015). We will, therefore, investigate the relationship between tau proteins and the development of these diseases.