Signalling and phosphorylation networks
Understanding the signalling mechanisms that co-ordinate cellular processes constitutes one of the core activities of the MCB theme. It has also been a central strand of the research strategy of the College where investment in proteomics, transgenics and imaging have provided a world class infra-structure that supports many of the cell signalling and protein phosphorylation based research programmes.
One of the current areas of excellence is to be found in G-protein coupled receptor (GPCR) research (Challiss, Herbert, Mahaut-Smith, Pullar, Willars, Willets, Tanaka, Tobin, Tincello). This has been a traditional strength for Leicester and one that forms the strategic focus for new funding in the near future (see below). Allied to this, is strength and depth in purinergic receptor research (Evans, Ennion, Vial, Goodall).
An emerging area of research has been an interest in phosphorylation networks. This originates in the long standing strength at Leicester of the investigation of cell growth via the MAP kinase family (Pritchard, Tanaka, Dickens) and nuclear division through the Nek kinases (Fry). Part of these research programmes are currently aimed at defining the mechanism of cell transformation in cancer by considering the impact of these kinase pathways on the global phospho-proteome. The ability to investigate this area has been made possible by substantial University investment into a core proteomic facility that can offer quantitative phospho-proteomic analysis.
The application of global phospho-proteomic approaches has also recently been applied to the first determination of the phospho-proteome of the human malarial parasite Plasmodium falciparum (Tobin). This work was funded by a £500K Wellcome project grant and now forms a central strategic initiative for the theme. Furthermore this technology is being applied to define the phospho-proteome and key protein kinase cascades in Tuberculosis Bacillus (O’Hare) and receptor tyrosine kinase signalling (Brindle).