Dr Debbie Cunningham PhD

Dr Debbie Cunningham

School of Biosciences
Assistant Professor in Molecular Cell Biology and Signalling

Contact details

507B, School of Biosciences
University of Birmingham
B15 2TT

Dr Cunningham is an expert in the use of quantitative proteomics techniques to characterise regulatory phosphorylation events and protein-protein interactions that occur during cell signalling.


PhD Biochemistry, University College London

BSc (Hons) Biomedical Sciences, University of Wolverhampton


Dr Cunningham began her scientific career in the pharmaceutical company Rhone-Poulenc Rorer, investigating the pharmacokinetics of novel compounds. She was then awarded a CASE award from the MRC to carry out a collaborative PhD at the National Institute of Medical Research, Mill Hill and GlaxoSmithKline during which she used biophysical techniques to investigate the enzymatic properties of a Rho GTPase-activating protein. Dr Cunningham remained at GlaxoSmithKline to carry out her first post-doctoral research position, developing assays to identify inhibitors of protein-protein interactions.

In 2002, Dr Cunningham came to the University of Birmingham to work in Professor John Heath’s lab investigating Fibroblast Growth Factor signalling in cancer. She is currently a Lecturer within the Molecules, Cells, Signalling and Health theme in the School of Biosciences and her research interests focus around the use of quantitative proteomics techniques to characterise cellular signalling networks.


BIO268 Cell and Developmental Biology (2nd year undergraduate)

BIO387 Cancer Biology (3rd year undergraduate)

BIOM26 Research Development and Funding (masters)

BIOM33 Regulatory Science and Toxicology for the 21st Century (masters)

Postgraduate supervision

Dr Cunningham is currently supervising four PhD students.

Dr Cunningham is interested in supervising doctoral research students in the following areas:

  • Characterisation of aberrant signalling events in cancer cells reliant on growth factor signalling for survival.
  • Understanding signalling pathways downstream of the metabolic fibroblast growth factor, FGF21.
  • Regulation of cellular metabolism by LAR phosphatase.

For possible PhD projects offered by Dr Cunningham please search FindAPhD.


In response to extra- and intra- cellular signals, post-translational modifications (PTMs) on proteins can be altered to modulate protein activity, stability, spatial localisation and interaction with other molecules. Phosphorylation is a key PTM involved in the transduction of cell signalling events, and aberrant phosphorylation is linked to human disease. Thus, a better understanding of the global phosphorylation events within a cell during signalling is crucial. A major focus of Dr Cunningham’s research is to obtain a ‘systems-wide’ understanding of phosphorylation events in signalling networks. Using state of the art mass spectrometry based proteomic techniques allows for a global analysis of pathway components and the changes in phosphorylation of these components on perturbation of the system. Stable isotope labelling by amino acids in cell culture (SILAC) coupled to high resolution mass spectrometry is used to identify global or targeted phosphorylation events, and protein-protein interactions that occur during signalling. Bioinformatic, biochemical and molecular cell biology methods techniques are used to investigate the functional relevance of regulated proteins and specific phosphorylation events identified from these quantitative proteomic experiments.

Growth Factor Signalling

Activation of signal transduction by the receptor tyrosine kinases, fibroblast growth factor receptor (FGFR) and platelet-derived growth factor receptor (PDGFR), results in a cascade of protein-protein interactions that rely on the occurrence of specific phosphorylation events. Unregulated activation of these receptors can lead to oncogenic manifestations in certain cell types. Utilising recent phosphoproteomics data, current research involves the study of novel proteins downstream of FGFR and PDGFR, and their role in regulating biological processes involved in cancer.

LAR Phosphatase

Leukocyte common antigen-related protein (LAR) is a member of the LAR subfamily of receptor-like protein tyrosine phosphatases (RPTPs). Recent proteomic and phosphoproteomic studies have significantly expanded our understanding of signalling events and biological processes downstream of LAR. Current research is aimed at further characterising the role of LAR in regulating cell adhesion and cellular metabolism.

ORCID identifier: 0000-0001-7776-690X http://orcid.org/0000-0001-7776-690X

Researcher ID: B-7329-2009 http://www.researcherid.com.ezproxyd.bham.ac.uk/rid/B-7329-2009

Other activities

Committee Membership

  • East Midlands Proteomics Workshop (EMPW)

Society Membership

  • Biochemical Society
  • British Society for Proteome Research
  • American Society for Mass Spectrometry


Selected Publications:

A complete publication list is available on Google Scholar: http://scholar.google.co.uk/citations?user=igC5IXQAAAAJ&hl=en

Sarhan, A.R., Patel, T.R., Cowell, A.R., Tomlinson, M.G., Hellberg, C., Heath, J.K., *Cunningham, D.L., and *Hotchin, N.A. (2016) LAR Protein Tyrosine Phosphatase Regulates Focal Adhesions via CDK1J Cell Sci 129(15), 2962-1971 (* joint senior authors)

Sarhan, A.R., Patel, T.R., Creese, A.J., Tomlinson, M.G., Hellberg, C., Heath, J.K., *Hotchin, N.A., *Cunningham, D.L. (2016) Regulation of Platelet Derived Growth Factor Signalling by LAR Protein Tyrosine Phosphatase: A Quantitative Phosphoproteomics Study Mol Cell Proteomics 15(6), 1823-1836 (* joint senior authors)

Zhao, H., Cunningham, D.L., Creese, A.J., Heath, J.K., and Cooper, H.J. (2015) FAIMS and phosphoproteomics of fibroblast growth factor signalling: Enhanced identification of multiply-phosphorylated peptides J Proteome Res 14, 5077-5087

Schoenherr, C., Serrels, B., Proby, C., Cunningham, D.L., Findlay, J.E., Baillie, G.S., Heath, J.K., and Frame, M.C. (2014) Epidermal growth factor receptor substrate 8 (Eps8) controls Src/Fak-dependent phenotypes in squamous carcinoma cells. J Cell Sci. J Cell Sci 127, 5303-5316

Jones, S., Cunningham D.L., Rappoport J.Z., and Heath J.K. (2014) The non-receptor tyrosine kinase Ack1 regulates activated EGFR fate by inducing trafficking to the p62/NBR1 pre-autophagosome. J Cell Sci 127, 994-1006

Cunningham D.L., Creese A.J., Auciello G., Sweet S.M.M., Tatar T., Rappoport J.Z., Grant M.M., and Heath J.K. (2013) Novel Binding Partners and Differentially Regulated Phosphorylation Sites Clarify Eps8 as a Multi-Functional Adaptor. PLoS ONE 8(4): e61513


Auciello, G., Cunningham, D. L. , Tatar, T., Heath, J. K., and Rappoport, J. Z. (2013) Regulation of fibroblast growth factor receptor signalling and trafficking by Src and Eps8. J Cell Sci 126, 613-624

Cunningham, D. L. , Sweet, S. M., Cooper, H. J., and Heath, J. K. (2010) Differential phosphoproteomics of fibroblast growth factor signaling: identification of Src family kinase-mediated phosphorylation events. J Proteome Res 9, 2317-2328

Sweet, S. M., Jones, A. W., Cunningham, D. L. , Heath, J. K., Creese, A. J., and Cooper, H. J. (2009) Database search strategies for proteomic data sets generated by electron capture dissociation mass spectrometry. J Proteome Res 8, 5475-5484

Bailey C.M., Sweet S.M., Cunningham D.L., Zeller M., Heath J.K.,Cooper, H.J. (2009) SLoMo: automated site localization of modifications from ETD/ECD mass spectra. J Proteome Res 8, 1965-1971

Sweet, S. M., Bailey, C. M., Cunningham, D. L., Heath, J. K., and Cooper, H. J. (2009) Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.  Mol Cell Proteomics 8, 904-912

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