The structure of microtubule-bound tau

Tau蛋白是一种神经元微管相关蛋白，它稳定微管并调节货物沿微管的运输。尽管在过去的几年里，密集的研究揭示了tau蛋白的功能及其在阿尔茨海默病中的作用，但仍然不清楚tau是如何与微管结合的。在这里，我建议用核磁共振波谱来表征微管结合的tau的结构性质。有关tau和微管之间相互作用的确切性质的信息至关重要，因为tau-微管相互作用的改变改变了与微管结合的tau部分与可溶性tau的平衡，并导致微管解聚和形成tau缠结，这一行为已被认为与大量神经退行性疾病有关。

The tau protein is a neuronal microtubule-associated protein which stabilizes microtubules and regulates the transport of cargo along microtubules. Although intense research has revealed much about the function of the protein tau and its involvement in Alzheimer's disease during the past years, it still remains unclear how tau binds to microtubules. Here I propose to characterize the structural properties of tau bound to microtubules using NMR spectroscopy. Information about the precise nature of the interactions between tau and microtubules is of central importance as altered tau-microtubule interactions change the balance in the fraction of tau bound to microtubules versus soluble tau and lead to depolymerisation of microtubules and formation tau tangles a behaviour that has been implicated in a large number of neurodegenerative diseases.