Prof Claire Eyers BSc, PhD

The major theme of my research career has been the development and application of biochemical and biophysical (mass spectrometry, ion mobility) techniques to study cellular signal transduction and post-translational modifications (PTMs), particularly protein phosphorylation, on a global level. Identification of PTMs ultimately leads to better understanding, and thus the ability to model, cell signalling systems. This is particularly pertinent as we try to define how changes in protein modification and cell signalling drives cellular ageing and the onset/progression of diseases. My research interests include the application of MS-based techniques to understand proteins and their modifications in a quantitative manner, both at the peptide and protein level, particularly to better understand the roles of combinatorial protein modifications. We also apply structural mass spectrometry (native IM-MS) to correlate changes in site-specific protein modification with protein conformational dynamics, complex formation and ligand (small molecule, DNA) binding.
I am currently funded by CRUK, NWCR, BBSRC and Unilever, and have been involved in a number of large-scale cross-disciplinary BBSRC (LOLA, SABR) and EU-funded projects, including:
i) absolute quantification of the complete proteome of S. cerevisiae (i.e. defining protein copy number per cell), and assessment of changes in protein cohorts under conditions of stress;
ii) in-depth characterisation of stimulation-dependent changes in the modification status of the NFκB transcription factor p65 in a temporal manner. By applying standard peptide-based quantitative phopshoproteomics, native structural mass spectrometry and novel strategies for intact protein (top down) proteomics that are currently being developed in my group, we are investigate the combinatorial roles of multiple modifications on individual NF-kB proteins as a function of disease (cancer) status and in response to stress stimuli;
iii) screening for cancer-associated changes in the serum glycome by developing novel MS-based methodology for capture and analysis of glycans, glycosylated proteins and glycan binding proteins using self-assembled monolayers;
iv) expanding the landscape of protein phosphorylation in human cells, having developed analytical strategies that allow sites of phosphorylation on non typical amino acids residues (e.g. His, Asp, Glu, Lys, Arg) to be defined.