Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates

Cantrelle, François-Xavier; Loyens, Anne; Trivelli, Xavier; Reimann, Oliver; Despres, Clément; S. Gandhi, Neha; P. R. Hackenberger, Christian; Landrieu, Isabelle; Smet-Nocca, Caroline

doi:10.3389/fnmol.2021.661368

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Phosphorylation and O-GlcNAcylation of the PHF-1 Epitope of Tau Protein Induce Local Conformational Changes of the C-Terminus and Modulate Tau Self-Assembly Into Fibrillar Aggregates

Shared by NobleBlocks on Jun 17, 2021 • 12:00 AM UTC

Authors:

François-Xavier Cantrelle

Anne Loyens

Xavier Trivelli

Abstract

Phosphorylation of the neuronal microtubule-associated Tau protein plays a critical role in the aggregation process leading to the formation of insoluble intraneuronal fibrils within Alzheimer’s disease (AD) brains. In recent years, other posttranslational modifications (PTMs) have been highlighted ...

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