Peter Parker

Protein Phosphorylation Laboratory

The development, propagation and spread of cancer are sustained by altered properties and inappropriate actions of normal physiological processes hijacked through the acquisition of genetic changes. Typically this involves gain or loss of function of particular gene products present in all of us and acting in the normal setting to effect highly orchestrated programmes of tissue maintenance, growth and regeneration in line with preserving normal tissue size and function.

Among the most widely engaged gene products in these physiological and pathological events are a family of over 500 multifunctional regulators, the protein kinases. These are some of the most frequently mutated gene products in cancer and many of the new, targeted therapeutics now in use in cancer treatments are directed at members of this protein kinase family.

In the context of cancer pathophysiology, we are working to understand how particular members of this protein kinase family act to drive properties particular to cancer - specifically, deregulated growth, survival and migration/invasion. Developing detailed molecular definitions of these events and assessing how the normal, physiological requirements for these kinases compare to the abnormal pathological requirements, provides evidence on the mechanisms and progression of disease, as well as biomarkers indicative of kinase action and insights into the potential value of intervention. Where appropriate, we have moved from these models to initiate collaborative drug development programmes, exploiting these insights to bring new agents into the clinic.

Selected publications

Linch, M., Sanz-Garcia, M., Rosse, C., Riou, P., Peel, N., Madsen, C. D., Sahai, E., Downward, J., Khwaja, A., Dillon, C., Roffey, J., Cameron, A. J., and Parker, P. J. (2014) Regulation of polarized morphogenesis by protein kinase C iota in oncogenic epithelial spheroids. Carcinogenesis 35, 396-406

Brownlow, N., Pike, T., Zicha, D., Collinson, L., and Parker, P. J. (2014) Mitotic catenation is monitored and resolved by a PKCepsilon-regulated pathway. Nat Commun 5, 5685

Riou, P., Kjaer, S., Garg, R., Purkiss, A., George, R., Cain, R. J., Bineva, G., Reymond, N., McColl, B., Thompson, A. J., O'Reilly, N., McDonald, N. Q., Parker, P. J., and Ridley, A. J. (2013) 14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteins. Cell 153, 640-653

Linch, M., Sanz-Garcia, M., Soriano, E., Zhang, Y., Riou, P., Rosse, C., Cameron, A., Knowles, P., Purkiss, A., Kjaer, S., McDonald, N. Q., and Parker, P. J. (2013) A cancer-associated mutation in atypical protein kinase Ciota occurs in a substrate-specific recruitment motif. Sci Signal 6, ra82

Rosse, C., Boeckeler, K., Linch, M., Radtke, S., Frith, D., Barnouin, K., Morsi, A. S., Hafezparast, M., Howell, M., and Parker, P. J. (2012) Binding of dynein intermediate chain 2 to paxillin controls focal adhesion dynamics and migration. J Cell Sci 125, 3733-3738

Peter Parker

peter.parker@crick.ac.uk
+44 (0)20 379 61977

  • Qualifications and history
  • 1979 PhD in Biochemistry, Oxford, UK
  • 1979 MRC Postdoctoral Fellowship, Dundee, UK
  • 1982 Postdoctoral Fellow, Imperial Cancer Research Fund, UK
  • 1985 Laboratory Head, Imperial Cancer Research Fund, UK
  • 1986 Laboratory Head, Ludwig Institute for Cancer Research, UK
  • 1990 Principal Investigator at the Imperial Cancer Research Fund, UK (in 2002 the Imperial Cancer Research Fund became Cancer Research UK)
  • 2006 Head of the Division of Cancer Studies King's College London, UK
  • 2015 Group Leader, the Francis Crick Institute, London, UK