Single-molecule imaging of Tau reveals how phosphorylation affects its movement and confinement in living cells.

ABSTRACT: Tau is a microtubule-associated protein that is regulated by post-translational modifications. The most studied of these modifications is phosphorylation, which affects Tau's aggregation and loss- and gain-of-functions, including the interaction with microtubules, in Alzheimer's disease and primary tauopathies. However, little is known about how Tau's phosphorylation state affects its dynamics and organisation at the single-molecule level. Here, using quantitative single-molecule localisation microscopy, we examined how mimicking or abrogating phosphorylation at 14 disease-associated serine and threonine residues through mutagenesis influences the behaviour of Tau in live Neuro-2a cells. We observed that both pseudohyperphosphorylated Tau (Tau^E14) and phosphorylation-deficient T

SUBMITTER: Padmanabhan P 

PROVIDER: S-EPMC10863257 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature