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Posttranslational modifications of amyloid proteins for proteasomal degradation


Dementia Research Institute

Applications accepted all year round Funded PhD Project (European/UK Students Only)

About the Project

PhD Studentship in the interplay between ubiquitin-proteasome degradation system and amyloid proteins, Imperial College London

Applications are invited for a 3.5 year PhD studentship in the UK DRI Centre at Imperial in the research group of Dr Yu Ye (https://www.imperial.ac.uk/people/yu.ye1).

The project is based at Imperial’s new White City Campus, the Hub for convergent research.

The UK Dementia Research Institute

There are currently around 850,000 people with dementia in the UK. This is projected to rise to 1.6 million by 2040. The UK DRI at Imperial has been established to address a medical research area of the highest importance and future impact. As one of seven national centres of excellence embedded in major UK universities, we intend to transform the diagnosis, treatment and care of people with dementias. The Medical Research Council and charity partners the Alzheimer's Society and Alzheimer’s Research UK have invested £290m in fulfilment of the ambition identified in the Prime Minister's 2020 Challenge on Dementia.

The laboratory

The fellowship programme of Dr Yu Ye is focused on the interplay between the ubiquitin-proteasome system (UPS) and amyloid proteins in biological systems. Using advanced fluorescence imaging techniques, the lab seeks to uncover the biochemical and cellular mechanisms of restricting or reversing protein aggregation, and how malfunction of the UPS system leads to neurodegenerative disorders.

Background

Posttranslational modifications on amyloid proteins have been shown to have critical roles involved in their aggregation behaviour. Enhanced phosphorylation and ubiquitination have been found in tau tangles in Alzheimer’s disease (AD) and Lewy Bodies in Parkinson’s disease (PD). Interestingly, ubiquitin moieties themselves are also prone to aggregation, further complicating the mechanisms through which toxic aggregates may assemble. In addition, both ubiquitinating (e.g. CHIP, Parkin) and deubiquitinating (e.g. USP14, USP9X) enzymes, as well as ubiquitin-dependent degradation through the proteasome, have been implicated in AD and PD. Understanding the key enzymatic activities that drive toxic protein aggregation is therefore critical to identify novel targets of therapeutic intervention to slow and reverse neurodegeneration.

The project

This PhD project is focused on studying posttranslational modifications on amyloids using biochemistry and cell biology approaches, with elements of advanced fluorescence imaging in live cells. The PhD candidate will enzymatically modify amyloid proteins, study how these proteins assemble into aggregates and at which aggregation stage they are prone to become posttranslationally modified. Using mass spectrometry and fluorescence microscopy, the candidate will further characterise additional factors involved in targeting the aggregates and the their level of toxicity to neuronal cells.

Studentship Details

Students will be registered in the Department of Brain Sciences in the Faculty of Medicine.
The award is for 42 months (full time) and covers course fees at the Home/EU rates (2020/21 fees £6,300 per annum) and a tax-free stipend starting at £19,000 per annum. Applicants must hold (or obtain by October 2020) a First Class or an Upper Second Class degree (or equivalent overseas qualification) in a Biological Sciences / Chemistry discipline, and Imperial would normally expect successful applicants to hold or achieve a Master's degree in a related field. Prior experience in ubiquitin-proteasome system is not essential but experience with biochemical and microscopy techniques would be preferred.
Non-EU applicants, if successful, will be responsible for payment of fees at the overseas rate (currently £39,600 per annum). Funding for overseas fees is not provided.

For informal enquiries please contact Dr Yu Ye (). For application, please send a full CV, stating your nationality, and the full contact details of two academic referees.
We regret that due to the large volume of applications received, we are only able to notify those shortlisted for interview. Applications will be considered throughout the year.

Funding Notes

The award is for 42 months (full time) and covers course fees at the Home/EU rates (2020/21 fees £6,300 per annum) and a tax-free stipend starting at £19,000 per annum.
Non-EU applicants, if successful, will be responsible for payment of fees at the overseas rate (currently £39,600 per annum). Funding for overseas fees is not provided.

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