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MSc by Research Programme: Deciphering the ubiquitin codes that regulate protein degradation


School of Life Sciences

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Dr Yogesh Kulathu No more applications being accepted Self-Funded PhD Students Only

About the Project

This course allows you to work alongside our world renowned experts from the School of Life Sciences and gain a ’real research’ experience. You will have the opportunity to select a research project from a variety of thematic areas of research.

You will be part of our collaborative working environment and have access to outstanding shared facilities such as microscopy and proteomics. Throughout your year, you will develop an advanced level of knowledge on your topic of interest as well as the ability to perform independent research in the topic area. Alongside basic science training in experimental design, data handling and research ethics, we will help you to develop skills in critical assessment and communication. This will be supported by workshops in scientific writing, presentation skills, ethics, laboratory safety, statistics, public engagement and optional applied bioinformatics.

The period of study is one year full-time or two years part-time research, which includes two months to write up the thesis. Please apply via the UCAS postgraduate application form: https://digital.ucas.com/courses/details?coursePrimaryId=c735d826-42b6-ca1f-50db-2a3ac6f68718


Ubiquitin signalling, which involves the posttranslational modification (PTM) of proteins with ubiquitin, regulates almost every aspect of eukaryotic biology. This versatility is possible because proteins can be modified with different types of ubiquitin codes resulting in distinct functional outcomes. An indispensable role for ubiquitylation is to serve as a signal for the degradation of misfolded and damaged proteins. In addition to degradation, ubiquitin modifications can serve as distinct signals to facilitate intracellular communication. The cellular machinery therefore has to read the different ubiquitin codes in order to ensure that the appropriate response is produced. Further, these codes have to be erased once the functional outcome is produced, a process carried out by a class of enzymes known as Deubiquitinases. In the lab we study these processes, using a range of techniques including biochemical approaches, proteomics, structural biology and mouse models to elucidate new layers of control in protein degradation. This research is fundamental to our understanding of cell biology in health, and is important, as failures in protein degradation underly many diseases especially age-related diseases such as Alzheimer’s and Parkinson’s disease.

We are looking for an enthusiastic student to join the group to study how protein degradation is regulated by the ubiquitin system. Your project will build upon tools, reagents and models we have recently established in the lab. Working on an independent project, you will have the opportunity to learn and apply different approaches ranging from biochemistry, cell biology, genetic screens and state-of-the-art proteomics methods to understand at the molecular level how aberrant proteins are degraded, the ubiquitin signals involved, how they are decoded and how this process is regulated. This project will provide the opportunity to improve our understanding of one of the most fundamental processes in the cell.
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