Abstract
Tau is a microtubule-associated protein, which facilitates the assembly and stability of neuronal microtubules in humans. Accumulation of tau into insoluble aggregates known as neurofibrillary tangles (NFTs) is a pathological hallmark of several neurodegenerative diseases. The current hypothesis is that small, soluble oligomeric tau species preceding NFT formation could be causing loss of tau function and toxicity. Here, using single molecule localization microscopy (SMLM), we show that, in vivo, tau forms small oligomers on microtubules under physiological conditions.
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