Absence of a Role for Phosphorylation in the Tau Pathology of Alzheimer's Disease.

ABSTRACT: Alzheimer's disease is characterized by redistribution of the tau protein pool from soluble to aggregated states. Aggregation forms proteolytically stable core polymers restricted to the repeat domain, and this binding interaction has prion-like properties. We have compared the binding properties of tau and tubulin in vitro using a system in which we can measure binding affinities for proteins alternated between solid and aqueous phases. The study reveals that a phase-shifted repeat domain fragment from the Paired Helical Filament core contains all that is required for high affinity tau-tau binding. Unlike tau-tubulin binding, tau-tau binding shows concentration-dependent enhancement in both phase directions due to an avidity effect which permits one molecule to bind to many as the concent

SUBMITTER: Lai RY 

PROVIDER: S-EPMC4919914 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature