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The University of Southampton
Biological Sciences

Research project: Unravelling the role of microtubule stabilisation in the pathogenesis of Alzheimer’s disease

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Project type: 
Studentship

Tau and Abeta are implicated in the pathogenesis of Alzheimer’s disease. The mechanisms by which they interact are unknown. This project focuses on exploring this.  Microtubule destabilisation is believed to be a key mechanism by which phosphorylated tau causes dysfunction in tauopathies. In Alzheimer’s disease Abeta peptide toxicity is mediated by phosphorylated tau. This PhD project investigates whether microtubule destabilisation underpins this tau-Abeta interaction.

Alzheimer's disease (AD) is the most common cause of cognitive decline in the elderly. It is characterised neuropathologically by amyloid-beta (A) peptide containing plaques and phospho-tau containing tangles. There is also evidence of loss of cytoskeletal integrity. This occurs as a result of loss of tau’s microtubule-stabilising function, caused by excessive disease-related hyper-phosphorylation. In trying to establish the relationship between plaques and tangles, many studies show that A-mediated learning and memory impairments require tau. One aim of this project is to investigate whether phospho-tau mediated cytoskeletal destabilisation underpins the cross talk between tau and A in a rodent model of AD. Another aim is to identify the mechanism of action of NAP, a peptide that counteracts phospho-tau’s microtubule defects and rescues phospho-tau phenotypes in a Drosophila model of AD. The outcomes of this project will enhance our understanding of the pathogenesis of AD and identify novel disease-modifying therapeutic targets.

Funding: The Gerald Kerkut Trust

Funding dates: 2015-2018

Affiliated research Groups: SONG, IFLS, Alzheimer Research Network

Related research groups

Biomedical Sciences
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