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Molecular analysis of the dynamic sulfotyrosine proteome

Institute of Integrative Biology

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Prof C E Eyers , Prof P Eyers , Dr A R Jones Applications accepted all year round Self-Funded PhD Students Only

About the Project

The survival of an organism depends upon the ability of different cell types to communicate with each other by assembling the correct complexes of proteins at the correct time in the correct place. One way this is achieved is by the addition of small chemical groups to proteins, as a means of regulating protein function, stability and/or cellular localisation. These events, termed ’post-translational modifications’ (PTMs), act as switches to change information flow and dictate the types of different biological outcomes elicited, such as cell movement, growth, survival or death. One such type of PTM, protein sulfation, is involved in the correct functioning of proteins inserted into membranes or destined for secretion. However, understanding the global significance of protein sulfation is challenging, since analysis has previously been difficult and there are few methods available to manipulate or study sulfation in a holistic manner.

This studentship will build on recently published findings from our groups (Byrne et al., 2018 Biochem J), which revealed that small molecule compounds that inhibit the cancer-driving protein kinase RAF also inhibit tyrosylprotein sulfotransferases (TPSTs), the enzymes that regulate tyrosine sulfation. Working alongside a team of BBSRC-funded researchers (led by Prof. Pat Eyers), this PhD project seeks to advance our understanding of the regulatory mechanisms and dynamics of cellular protein sulfation, gaining unique insight into how this understudied PTM regulates both cellular and extracellular biology in health and disease.

Specifically, the studentship will develop, and then apply, cutting-edge mass spectrometry-based proteomics techniques to explore protein sulfation and to characterize the effects of clinically approved small molecule enzyme inhibitors on protein sulfation in cells. Ultimately, this knowledge will lead to better understanding of basic sulfation biology, but will potentially also improve clinical outcomes arising as a result of more detailed characterisation of the cellular effects of chemotherapeutics that change protein sulfation.

The studentship will be based in the Department of Biochemistry in the Institute of Integrative Biology at the University of Liverpool, working primarily in the Centre for Proteome Research under the supervision of Prof. Claire Eyers, in close collaboration with Prof. Andy Jones and Prof. Pat Eyers, who will provide additional training and expertise in computational biology and biochemistry/chemical biology relevant to the project.
The project is suited to a student with (at least) a good Upper Second B.Sc. in Biochemistry, Chemistry or related discipline, ideally with a strong background in the molecular basis of cell signalling.

Funding Notes


Eligibility: Applicant requires an Upper Second B.Sc. (or equivalent) in Biochemistry, Chemistry or related discipline.
Start date: Open
4 year PhD programme


Byrne D, Li Y, Ngamlert P, Ramakrishnan K, Eyers C, Wells C, Drewry D, Zurcher W, Berry N, Fernig D, Eyers P. New tools for evaluating protein tyrosine sulfation: TPSTs are novel targets for RAF protein kinase inhibitors. Biochem J. 2018 475:2435
Ferries S, Perkins S, Brownridge PJ, Campbell A, Eyers PA, Jones AR and Eyers CE. Evaluation of Parameters for Confident Phosphorylation Site Localization using an Orbitrap Fusion Tribrid Mass Spectrometer. J Prot Research (2017) 16 (9), 3448–3459.
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