Journal Article (Review Article)

DZNE-2021-00309

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png A current view on Tau protein phosphorylation in Alzheimer's disease.

Wegmann, S. (First author)DZNE* ; Biernat, J.DZNE* ; Mandelkow, E. (Last author)DZNE*

2021
Current Biology Philadelphia, Pa.

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Please use a persistent id in citations: doi:10.1016/j.conb.2021.03.003

Abstract: 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. However, the phosphorylation patterns of physiological and pathological Tau are surprisingly similar and heterogenous, making it difficult to identify specific modifications as therapeutic targets and biomarkers for AD. We present a concise summary of - and view on - important previous and recent advances in Tau phosphorylation analysis in the context of AD.

Keyword(s): Alzheimer Disease (MeSH) ; Humans (MeSH) ; Phosphorylation (MeSH) ; Protein Processing, Post-Translational (MeSH) ; Tauopathies (MeSH) ; tau Proteins: metabolism (MeSH)

Note: funding grant > DFG SPP2191

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Contributing Institute(s):

1. Protein Actions in Neurodegeneration (AG Wegmann)
2. Structural Principles of Neurodegeneration (AG Mandelkow 1 ; AG Mandelkow 1)

Research Program(s):

1. 352 - Disease Mechanisms (POF4-352) (POF4-352)

Appears in the scientific report 2021

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