Under physiologicalconditions, tau binds to tubulin and stabilizes microtubules, thusplaying a critical role in neuron morphology, axon development, andnavigation.1 In its native conformation,tau is largely unfolded, highly disordered, and stable.2 However, in the numerous neuropathologies knownas tauopathies, tau is aggregated into amyloid fibrils, which in turnmay produce severe pathologies known as protein misfolding diseases.The most-prevalent tauopathy is Alzheimer’s disease (AD), whichseverely damages the cognitive function of the elderly and threatenstheir health.3 The gene discussed is MAPT; the disease is proteostasis deficiencies.