Kathryn was always set on a career in science and carried out a degree in Biochemistry at the University of Salford where she became captivated by classical chemistry and protein structure-function. After receiving her degree Kathryn moved to the Biochemistry Department at the University of Leeds and decided to do a PhD that combined her interests by studying the mechanism by which the enzyme lipoprotein lipase was degraded. This set her on a path as an enzymologist and she subsequently won a Broodbank Fellowship to study the regulation of pyrophosphate-fructose-6-phosphate 1-phosphotransferase in the laboratory of Prof Tom ap Rees at the University of Cambridge. Tom was a stickler for quantification and strongly believed that his interactions with students and the members of his group should always come before administrative tasks. Although Tom’s life was sadly cut short in a road accident (in 1996) he has continued to be a role model and inspiration to Kathryn throughout her career. She moved on to do post-doctoral studies at Michigan State University (Moo-U!) in the USA before returning to the UK to learn about the enzymology of protein kinases in Dundee. It was whilst at the University of Dundee that Kathryn started to work on the structure, function and post-translational regulation of proteins/enzymes involved in tumour suppression and cell growth control with Prof Sir David Lane. It was David’s encouragement of an eclectic approach to address scientific questions which inspired Kathryn to take a more cross-disciplinary approach to her research. Whilst in Dundee Kathryn was awarded first a Project Grant and then a CRUK Senior Cancer Research Fellowship to establish her own group studying the post-translational regulation of the growth regulator p21WAF1. Using p21WAF1 as a starting point the Ball lab moved into the field of Interferon Regulated Transcription Factors. Kathryn moved her group to the University of Edinburgh in 2004 to take up a Readership and to set-up a cross-disciplinary programme of research that uses Biophysics and Chemistry as well as Biochemistry and cell systems to study IRF-1 regulation and the mechanism of ubiquitination by E3-ubiquitin ligases. Kathryn was awarded a personal chair (Biochemistry and Cell Signalling) in 2007, however she still likes to get into the lab, especially if it involved protein purification, as she has a great view of Edinburgh castle from her bench.

RF-1 is an interferon regulated transcription factor with roles in a diverse range of growth control and immunological processes. These processes include apoptosis, cell cycle control, antigen presentation, differentiation and the response to pathogen infection. In addition IRF-1 is a component of an intrinsic tumour suppressor network that acts to defend the cell from oncogenic stimuli or from disruption of its genetic material. The loss of IRF-1 function is associated with the development of cancers of the breast and GI tract, as well as a wide variety of leukaemias. Interestingly however decreased IRF-1 expression enhances resistance to HIV infection whereas elevated levels of the protein can promote autoimmune diseases. IRF-1 therefore represents a potential therapeutic target as it controls a cohort of genes with fundamental roles in human health and disease.  However it is currently impractical to design IRF-1 targeted therapies as we know relatively little about how the protein is regulated at the post-translational level and whether deficiencies in the enzymes and protein which form the IRF-1 interactome can enhance or impede the development of human pathologies. This has driven the Ball group to focus their research on defining the intrinsic and extrinsic mechanisms that control IRF-1 protein function.

The group have recently discovered that the post-translational regulatory network controlling IRF-1 function and turnover is rate-limiting for the modulation of downstream genes involved in immunity and tumour suppression. In order to capitalise on this they are using a cross-disciplinary approach to study IRF-1 structure in relation to its turnover, modification by ubiquitin, regulation by reversible phosphorylation and biological function(s). They are also combining biochemistry with biophysics, chemistry and cell biology in order to develop novel biologics and small molecules which can be used to study the regulation of endogenous IRF-1 pathway components and to link them to physiological outcome using chemical genetics. To ensure the success of their research programme the Ball group are actively involved in a number of exciting local and international collaborations which give access to expertise in protein structure and biophysics, dynamic protein modelling, state of the art mass spectrometry and chemistry. In addition, they interact with molecular immunologists and clinical collaborators to gain insight into human health and disease.