EB1 Increases the Dynamics of Tau Droplets and Inhibits Tau Aggregation: Implications in Tauopathies.

EB1, a microtubule plus end-tracking protein (+TIP), regulates microtubule dynamics. Recent evidence indicates cross-talk between EB proteins and tau, a microtubule-associated neuronal protein that is important for the growth and stability of microtubules. We investigated the interaction between tau and EB1 and the effect of binding of EB1 on tau function and aggregation.

Shikonin impedes phase separation and aggregation of tau and protects SH-SY5Y cells from the toxic effects of tau oligomers.

Tauopathies such as Alzheimer's and Parkinson's diseases involve the abnormal deposition of tau aggregates in the brain and neuronal tissues. We report that a natural naphthoquinone, shikonin, impeded the oligomerization and fibrillization of tau. The compound strongly inhibited heparin, arachidonic acid, and RNA-induced tau aggregation.

Regulation of neuronal microtubule dynamics by tau: Implications for tauopathies.

In specialized cell types such as neurons, microtubules maintain the integrity of axons by forming stable bundles and facilitate the transport of synaptic vesicles. The cells regulate the stability and dynamics of microtubules using a diverse array of mechanisms. One of the mechanisms involves the interaction of microtubules with its associated proteins.