Abstract
Tau is a neuron-specific microtubule-binding protein that stabilizes microtubules. It is generally thought that highly phosphorylated tau dissociates from microtubules and becomes insoluble aggregates, leading to neuronal degeneration. Due to the implication of tau aggregation in neurodegenerative disorders, including Alzheimer’s disease, great efforts have been made to identify the tau aggregation process. However, tau interaction with tubulin during the aggregation process remains largely unknown. To scrutinize the tau-tubulin interaction, we generated a cell model that enables visualization of the tau-tubulin interaction in a living cell using the Bifluorescence Complementation (BiFC) Technique. Upon diverse chemical stimulation that induced tau pathology, tau-tubulin BiFC cells showed significantly increased levels of BiFC fluorescence, indicating that tau aggregates together with tubulin. Our results suggest that tubulin should be considered as a key component in the tau aggregation process.
Highlights
Tau is a neuron-specific microtubule-associated protein that promotes microtubule assembly and stabilization in healthy neurons [1,2]
Neuronalstructure structureand andaxon axonstability stability rely on built byby microtubules, Neuronal on the thecytoskeleton cytoskeletonframework framework built microtubules, which are polymers that vary in length and are composed of tubulin subunits
Tau bindstau which are polymers that vary in length and are composed of tubulin subunits
Summary
Tau is a neuron-specific microtubule-associated protein that promotes microtubule assembly and stabilization in healthy neurons [1,2]. A recent study showed that FTDP-17-associated tau mutants have a strong binding affinity with tubulin dimers [9], suggesting that tubulin may play a role in the pathological tau aggregation. Avila group reported that β-tubulin participates in the formation of tau aggregates in neurofibrillary tangles (NFTs) and Pick bodies [10]. To scrutinize tau-tubulin interactions under conditions, a cell-based livingthat cellscan would be a useful tool. Tau-tubulin interactions in living cells would be a useful tool. The fluorescence intensities in the cytoplasm total tubulin-BiFC cells. We generated chemical and environmental stimuli that trigger tau pathology [15,16,17]. We generated the tau-tubulin BiFC cell line to visualize tau-tubulin interaction in a living cell and investigated tau-tubulin interaction upon the activation of tau pathology
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