Microtubule-associated protein tau, pathologically phosphorylated form (Tau (pathological/p-tau or pTau))

Pathologically phosphorylated tau refers to the abnormally and excessively phosphorylated form of microtubule-associated protein tau. Under normal conditions, tau stabilizes neuronal microtubules, supporting cytoskeletal structure and axonal transport. In neurodegenerative disease, particularly Alzheimer's disease, tau becomes hyperphosphorylated at multiple serine and threonine residues. This pathological modification reduces tau's affinity for microtubules, leading to cytoskeletal destabilization, mislocalization, and formation of insoluble aggregates such as paired helical filaments (PHFs) and neurofibrillary tangles[2][3][4][5][6][7]. These tau aggregates disrupt neuronal function, contribute to mitochondrial and synaptic dysfunction, and drive neuronal death. Pathologically phosphorylated tau is a key biomarker and therapeutic target in “tauopathies,” with research ongoing into immunotherapies and kinase-modulating drugs. Monitoring CSF phosphorylated tau species is central to Alzheimer's disease diagnosis and progression tracking.

Other names

Tau protein (hyperphosphorylated)pathological taupTauhyperphosphorylated tauPHF-taupaired helical filament tauneurofibrillary tauAD P-tau

Antibody-mediated clearance or neutralization of pathological tau species[1][5]; Inhibition of kinases responsible for tau phosphorylation (e.g., GSK3β, Cdk5 inhibitors)[6]; Enhancement of phosphatase-mediated dephosphorylation (experimental)