About the Project
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
Ubiquitylation represents a major post-translational modification that controls numerous cellular processes. In the course of our research studies into Parkinson’s disease mechanisms, we discovered that ubiquitin itself can be modified by phosphorylation. In mammalian systems the PINK1 kinase phosphorylates ubiquitin at residue Serine65 (Ser65) and this Ser65 -Phospho-ubiquitin functions as a chemical messenger to activate the Parkinson’s ubiquitin ligase, Parkin. Global mass spectrometry screens have provided evidence that ubiquitin can be phosphorylated at other residues in cells and tissues derived from various human cancers. The regulation of these other Phospho-ubiquitin species including the identity of their upstream kinases is unknown and their significance in human disease states unclear. The development of tools is a critical next step and we have recently generated state-of-the-art phospho-specific antibodies against all known ubiquitin phosphorylation sites (Thr7, Thr12, Thr14, Ser20, Ser57, Tyr59, Ser65 and Thr66). The project seeks to determine the biological role of these Phospho-ubiquitin species in cells. Specifically we will deploy these anti-Phospho-ubiquitin antibodies in cells stimulated by diverse stimuli including growth factor stimulation, mitogen activation and DNA-damaging induced stimuli. cellular studies to better understand their regulation in signalling pathways linked to cancer. Where a specific stimulus is identified to induce Phospho-ubiquitin, appropriate follow-up studies will be undertaken to define the regulatory mechanism including the identification of the kinase. The project will also involve a collaboration with the Tayside Biorepository to validate the role of specific Phospho-ubiquitin species in cells and tissues derived from various cancers.
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