Tau protein phosphorylated at threonine-217 (Tau pT217)

Tau protein phosphorylated at threonine-217 (Tau pT217) is a post-translationally modified form of tau, a microtubule-associated protein highly expressed in neurons, where it stabilizes microtubules and regulates axonal transport[1][2][3]. Phosphorylation at threonine-217 alters tau’s normal function and reduces its microtubule-binding affinity, contributing to microtubule destabilization and impaired axonal transport[1][6]. In neurodegenerative diseases such as Alzheimer’s disease (AD), Tau pT217 is an early-appearing pathological species that promotes tau aggregation and formation of neurofibrillary tangles, key features of tauopathies[4][5][7]. Tau pT217 in CSF and plasma is a highly promising early biomarker for AD, correlating with disease pathology and discriminating AD from other neurodegenerative disorders[4][6][8]. It is under active consideration as a therapeutic target, particularly for immunotherapeutic strategies aimed at clearing pathogenic tau or inhibiting its aggregation, though no direct targeting drugs are yet clinically approved[7]. Key challenges include preserved physiological tau functions and ensuring specificity for pathological tau species.

Other names

Tau pT217phosphorylated tau 217pThr217 tautau protein pT217

Immunotherapy: Antibodies binding to phosphorylated tau (potentially including pT217) to promote its clearance or prevent its spread; Restriction of tau aggregation: Modifying kinase activity to reduce phosphorylation at pathogenic sites (experimental); Ubiquitin ligase modulation: Interference with pathological protein interactions (e.g., CTLH E3 ubiquitin ligase complex[5])