The functions of the neuronal microtubule-associated protein Tau in the central nervous system are regulated by manifold posttranslational modifications at more than 50 sites. Tau in healthy neurons carries multiple phosphate groups, mostly in its microtubule assembly domain. Elevated phosphorylation and aggregation of Tau are widely considered pathological hallmarks in Alzheimer's disease (AD) and other tauopathies, triggering the quest for Tau posttranslational modifications in the disease context [PMID: 33892381]. Tau phosphorylation at Thr231 can be detected in cerebrospinal fluid and shows potential as a biomarker of neurofibrillary pathology in Alzheimer’s disease [PMID: 17012293].
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