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      Prof Stephen Dilworth

      ROLE: Hourly Academic
      SCHOOL: Science & Technology
      DEPARTMENT: Natural Sciences
      TELEPHONE: +44 (0)20 8411 4338
      EMAIL: S.Dilworth@mdx.ac.uk
      1. Biography &
        Qualifications
      2. Learning &
        Teaching Interests
      3. Research Outputs &
        Interests
      4. Funded Research &
        Knowledge Exchange Projects
      5. Engagement &
        Impact

      • Biography &
        Qualifications

        Stephen Dilworth joined Middlesex University in September 2010 as Professor of Cancer Biology. He gained his first degree and a Masters in Natural Sciences from St Johns College Cambridge, and then a PhD from Imperial College, London University. His thesis work was conducted at the Imperial Cancer Research Fund in London, from where he moved back to Cambridge University as a Research Associate for six years. He then joined the Royal Postgraduate Medical School in London (the RPMS, later merged into the Imperial College School of Medicine) as a Lecturer, where he established his own research group, and advanced to a Reader in Tumour Virology.

        Stephen's research work has focussed on identifying the essential changes that occur in cells as they become cancerous. This started with his PhD work studying the oncogenic viral proteins made by the mouse polyoma virus, to which he returned when setting up his own group at the RPMS. During his 30 years working in this area, he isolated the first monoclonal antibodies directed against these viral proteins, and isolated a number of proteins that interact with the middle T-antigen, including a tyrosine phosphorylated protein that was later identified as an essential component of the mechanism used by tumour cells to avoid programmed cell death. His group also identified the ShcA protein as a middle T binding protein which led to the realisation that MT acts in the same way as a cell growth factor receptor, a key discovery in unravelling how receptors act in human cancer formation. His work continues in this area, but he has also made significant contributions in the field of cell nucleus assembly, including chromatin formation, and the signals that specify proteins to accumulate within the nucleus. Many of the antibodies made by his group are currently used in cancer screening assays.

        Education and Qualifications

        1968-1974Marsh Hill Boy's Grammar School, Birmingham
        1973 

        A-Levels. 3 grade A, 1 grade B. (Biology, Chemistry, Physics and Mathematics)

        1975-1978St. John's College, Cambridge. B.A. (Hons.) Class: First.
        Subject: Natural Sciences
        1981M.A.
        1978 - 1982External PhD Student, Imperial College, London
        1983P.H.D. Thesis title: Polyoma virus T-antigens. 
        Work performed at ICRF, LIF Branch.

        Languages Spoken

      • Learning &
        Teaching Interests

      • Research Outputs &
        Interests

        At ICRF I characterised the T-antigens encoded by polyoma virus. I helped mapg the coding regions used to synthesise each protein, and produced the first monoclonal antibodies (MAbs) directed against the T-antigens. I then used these MAbs to characterise the MT-kinase complex and the polypeptides phosphorylated by the activity. This was an important pre-requisite to identifying both pp60c-srcand PI3K associated with MT. The MAbs also allowed us to perform direct sub-cellular location studies on MT for the first time. Finally, the MAbs were used to purify sufficient large T-antigen to allow biochemical characterisation of its DNA binding activity.

        A change in scientific direction followed in a move to Cambridge where the molecular mechanisms behind the replication and assembly of the eukaryotic nucleus were studied. I isolated a series of MAbs directed against the components of chromatin assembly in X.laevisembryos, and used these to define the complexes involved in producing nucleosomes during development. These antibodies were then used to examine further aspects of chromatin assembly, including the role of H1 analogues, and chromatin decondensation. I was also part of the team that cloned the nucleosome assembly factor, nucleoplasmin, and identified and characterised the now canonical bi-partite nuclear migration sequence.

        In 1988 I moved to the RPMS in London, and established my own research group returning to the investigation of the transforming action of the middle T-antigen of polyoma virus. New MAbs have generated a comprehensive antigenic map of MT which was used to identify, and define the molecular characteristics of a novel pp60c-src binding site in MT through development of an in vitro system that recreates the complete MT complex within the test tube. This has led to the definition of the sequences in pp60c-src that are recognised by MT.

        Some of our main achievements have been through the identification of new MT binding proteins, including the ShcA polypeptides. We used our MAbs to establish the binding site on MT for Shc, then characterised the consequences of this interaction, which involve the phosphorylation of Shc, binding Grb2 and mSos, and activation of p21ras, and the MAP Kinase cascade. This was instrumental in our realisation of the now generally accepted fact that MT was mimicking the actions of tyrosine kinase associated growth factor receptors. We have been able to use MT as a receptacle for other tyrosine containing sequences, and have used this system to establish how the important phosphorylation sites in ShcA function in both transformation and differentiation induction. This identified another new MT associated protein in Gab1. Current work involves characterising the membrane location sequence in MT and defining the requirements for cellular transformation. MT has been found to be located in discrete complexes on the cell membrane, and this localisation is essential for transformation.

        Publications

        1. Novak, U., Dilworth, S.M., and Griffin, B.E. (1980). Coding capacity of a 35% fragment of the polyoma virus genome is sufficient to initiate and maintain cellular transformation. Proc. Natl. Acad. Sci. USA. 77 3278-3282.
        2. Magnusson, G., Nilsson, M.G., Dilworth, S.M., and Smolar, N. (1981). Characterization of Polyoma Mutants with Altered Middle and Large T-Antigens. Virol. 39 673-683.
        3. Dilworth, S.M., and Griffin, B.E. (1982). Monoclonal antibodies against polyoma virus tumor antigens. Proc. Natl. Acad. Sci. USA. 79 1059-1063.
        4. McCormick, F., Lane, D.P., and Dilworth, S.M. (1982). Immunological Cross-Reaction between Large T-Antigens of SV40 and Polyoma Virus. Virology 116 382-387.
        5. Dilworth, S.M. (1982). Protein kinase activities associated with distinct antigenic forms of polyoma virus middle T-antigen. EMBO Jl. 1 1319-1328.
        6. Ding, D.M., Dilworth, S.M., and Griffin, B.E. (1982). mlt Mutants of polyoma virus. J. Virol. 44 1080-1083.
        7. Dilworth, S.M., Cowie, A., Kamen, R.I., and Griffin, B.E. (1984). DNA binding activity of polyoma virus large tumor antigen. Proc. Natl. Acad. Sci. USA. 81 1941-1945.
        8. Dilworth, S.M., Hansson, H.A., Darnfors, C., Bjursell, G., Streuli, C.H., and Griffin, B.E. (1986). Subcellular localisation of the middle and large T-antigens of polyoma virus. EMBO Jl. 5 491-499.
        9. Dingwall, C., Dilworth, S.M., Black, S.J., Kearsey, S.E., Cox, L.S., and Laskey, R.A. (1987). Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a  cluster of sequences homologous to putative nuclear localization signals. EMBO Jl. 6 69-74.
        10. Dilworth, S.M., Black, S.J., and Laskey, R.A. (1987). Two Complexes That Contain Histones Are Required for Nucleosome Assembly In Vitro: Role of Nucleoplasmin and N1 in Xenopus Egg Extracts. Cell 51 1009-1018.
        11. Richardson, W.D., Mills, A.D., Dilworth, S.M., Laskey, R.A., and Dingwall, C. (1988). Nuclear Protein Migration Involves Two Steps: Rapid Binding at the Nuclear Envelope Followed by Slower Translocation through Nuclear Pores. Cell 52 655-664.
        12. Dingwall, C., Robbins, J., Dilworth, S.M., Roberts, B., and Richardson, W.D. (1988). The Nucleoplasmin Nuclear Location Sequence Is Larger and More Complex than That of SV 40 Large T Antigen. J. Cell Biol. 107 842-849.
        13. Lane, N.J., and Dilworth, S.M. (1989). Isolation and biochemical characterization of septate junctions: differences between the proteins in smooth and pleated varieties. J. Cell Sci. 93 123-131.
        14. Blanco, J., Millstein, L., Razik, M.A., Dilworth, S.M., Cote, C., and Gottesfeld, J. (1989). Two TF IIIA activities regulate expression of the Xenopus 5S gene families. Genes and Development. 3 1602-1612.
        15. Dingwall, C., Robbins, J., and Dilworth, S.M. (1989). Characterisation of the nuclear location sequence of Xenopus nucleoplasmin. J. Cell Sci. Suppl. 11 243-248.
        16. Dilworth, S.M. (1991). A perichromosomal region contains proteins phosphorylated during mitosis in Xenopus laevis cells. J. Cell Sci. 98 309-315.
        17. Robbins, J., Dilworth, S.M., Laskey, R.A., and Dingwall, C. (1991). Two Interdependent Basic Domains in Nucleoplasmin Nuclear Targeting Sequence: Identification of a Class of Bipartite Nuclear Targeting Sequence. Cell 64 615-623.
        18. Hopwood, N.D., Pluck, A., Gurdon, J.B., and Dilworth, S.M. (1992). Expression of XMyoD in early Xenopus laevis embryos. Development. 114 31-38.
        19. Forstova, J., Krauzewicz, N., Wallace, S., Street, A.J., Dilworth, S.M., Beard, S., and Griffin, B.E. (1993). Cooperation of Structural Proteins During Late Events in the Life Cycle of Polyoma Virus. J. Virol. 67 1405-1413.
        20. Dilworth, S.M., and Horner, V.P. (1993). Novel Monoclonal Antibodies That Differentiate Between the Binding of pp60c-src or Protein Phosphatase 2A by Polyoma Virus Middle T-Antigen. J. Virol. 67 2235-2244.
        21. Dilworth, S.M., Brewster, E.P., Jones, M.D., Lanfrancone, L., Pelicci, G., and Pelicci, P.G. (1994). Transformation by polyoma virus middle T-antigen requires the binding and tyrosine phosphorylation of Shc. Nature 367 87-90.
        22. Messerschmitt, A., Disela, C., Dilworth, S., Marti, A.G., and Ballmer-Hofer, K. (1996). Polyomavirus middle-T antigen lacking a membrane anchor sequence accumulates in the nucleus. J. Gen. Virol. 77. 17-26.
        23. Brewster, C.E.P., Glover, H.R., and Dilworth, S.M. (1997). Pp60c-src Binding to Polyomavirus Middle T-Antigen (MT) Requires Residues 185 to 210 of the MT Sequence. J. Virol. 71 5512-5520.
        24. Blaikie, P.A., Fournier, E., Dilworth, S.M., Birnbaum, D., Borg, J-P, and Margolis, B. (1997). The Role of the Shc Phosphotyrosine Interaction/Phosphotyrosine Binding Domain and Tyrosine Phosphorylation Sites in Polyoma Middle T Antigen-mediated cell transformation. J. Biol. Chem. 272 20671-20677.
        25. Senften, M., Dilworth, S., and Ballmer-Hofer, K. (1997). Multimerization of the Polyomavirus Middle-T Antigen. J. Virol. 71 6990-6995.
        26. Kennedy, A.P., Sekulic, A., Irvin, B.J., Nilson, A.E., Dilworth, S.M., and Abraham, R.T. (1998). Polyomavirus-Derived Middle-T Antigen as a Probe for T-Cell Antigen Receptor-Coupled Signalling Pathways. J. Biol. Chem. 273 11505-11513.
        27. Glover, H.R., Brewster, C.E.P., and Dilworth, S.M. (1999). Association Between src-kinases and the Polyoma Virus Oncogene Middle T-antigen Requires PP2A and a Specific Sequence Motif. Oncogene. 18 4364-4370.
        28. Abraham, D., Podar, K., Pacher,M., Kubicek, M., Welzel, N., Hemmings, B.A., Dilworth, S.M., Mischak, H., Kolch, W., and Baccarini, M. (2000). Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation. J Biol Chem. 275 22300-22304.
        29. Nicholson, P.R., Empereur, S., Glover, H.R., and Dilworth, S.M. (2001). ShcA tyrosine phosphorylation sites can replace ShcA binding in signalling by middle T-antigen. EMBO J. 20 6337-6346.
        30. Ong, S.H., Dilworth, S., Hauck-Schmalenberger, I., Pawson, T., and Kiefer, F. (2001). ShcA and Grb2 mediate polyoma middle T antigen-induced endothelial transformation and Gab1 tyrosine phosphorylation. EMBO J. 20 6327-6336
        31. Meng, M.V., Grossfeld, G.D., Williams, G.H., Dilworth, S., Stoeber, K., Mulley, T.W., Weinberg, V., Carroll, P.R., and Tlsty, T.D. (2001). Minichromosome maintenance protein 2 expression in prostate: characterization and association with outcome after therapy for cancer. Clin-Cancer-Res. 7 2712-2718.
        32. Mukherjee, G., Freeman, A., Moore, R., Kumaraswamy, Devi, K.U., Morris, L.S., Coleman, N., Dilworth, S., Prabhakaran, P.S., and Stanley, M.A. (2001). Biologic factors and response to radiotherapy in carcinoma of the cervix. Int-J-Gynecol-Cancer. 11 187-193
        33. Srivastava, J., Goris, J., Dilworth, S.M., and Parker, P.J. (2002). Dephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotides. FEBS-Lett. 516 265-269.
        34. Davies, R.J., Freeman, A., Morris, L.S., Bingham, S., Dilworth, S., Scott, I., Laskey, R.A., Miller, R., and Coleman, N. (2002). Analysis of minichromosome maintenance proteins as a novel method for detection of colorectal cancer in stool. The Lancet. 359 1917-1919.
        35. Stoeber, K., Swinn, R., Prevost, T., Clive-Lowe, P., Halsall, I., Dilworth, S.M., Marr, J., Turner, W.H., Bullock, N., Doble, A., Hales, C.N. and Williams, G.H. (2002). Diagnosis of genito-urinary tract cancer by detection of minichromosome maintenance 5 protein in urine sediments. J. Natl. Cancer Inst. 94 1071-1079.
        36. Stevens, I., Janssens, V., Martens, E., Dilworth, S., Goris, J., and Van Hoof, C. (2003). Identification and characterization of B"-subunits of protein phosphatase 2 A in Xenopus laevis oocytes and adult tissues. Eur. J. Biochem., 270 376-387.
        37. Horman, S., Hussain, N., Dilworth, S.M., Storey, K.B., and Rider, M.H. (2005). Evaluation of the role of AMP-activated protein kinase and its downstream targets in mammalian hibernation. Comparative biochemistry and physiology142, 374-382.
        38. Lampert, I.A., Horncastle, D., Dilworth, S., Roberts, I., Alison, M.R., and Naresh, K.N. (2005). The expression of minichromosome maintenance protein-2 in normal and abnormal megakaryocytes and comparison with the proliferative marker Ki-67. British journal of haematology131, 490-494.
        39. Pim, D., Massimi, P., Dilworth, S.M., and Banks, L. (2005). Activation of the protein kinase B pathway by the HPV-16 E7 oncoprotein occurs through a mechanism involving interaction with PP2A. Oncogene24, 7830-7838.
        40. Rider, M.H., Hussain, N., Horman, S., Dilworth, S.M., and Storey, K.B. (2006). Stress-induced activation of the AMP-activated protein kinase in the freeze-tolerant frog Rana sylvatica. Cryobiology53, 297-30
        41. Stubbs, S.A., Stark, J., Dilworth, S.M., Franks, S., and Hardy, K. (2007). Abnormal preantral folliculogenesis in polycystic ovaries is associated with increased granulosa cell division. J Clin Endocrinol Metab92, 4418-4426.
        42. You, Z., Bailis, J.M., Johnson, S.A., Dilworth, S.M., and Hunter, T. (2007). Rapid activation of ATM on DNA flanking double-strand breaks. Nat Cell Biol9, 1311-1318.
        43. Kiskinis, E., Hallberg, M., Christian, M., Olofsson, M., Dilworth, S.M., White, R., and Parker, M.G. (2007). RIP140 directs histone and DNA methylation to silence Ucp1 expression in white adipocytes. EMBO J26, 4831-4840.
        44. Hallberg, M., Morganstein, D.L., Kiskinis, E., Shah, K., Kralli, A., Dilworth, S.M., White, R., Parker, M.G., and Christian, M. (2008). A functional interaction between RIP140 and PGC-1alpha regulates the expression of the lipid droplet protein CIDEA. Mol Cell Biol28, 6785-6795.
        45. Rider, M.H., Hussain, N., Dilworth, S.M., and Storey, K.B. (2009). Phosphorylation of translation factors in response to anoxia in turtles, Trachemys scripta elegans: role of the AMP-activated protein kinase and target of rapamycin signalling pathways. Mol Cell Biochem. 332, 207-213.
        46. Atkin, S. J., Griffin, B. E. and Dilworth, S. M. (2009) Polyoma virus and simian virus 40 as cancer models: history and perspectives. Semin Cancer Biol. 19, 211-217
        47. Rider, M. H., Hussain, N., Dilworth, S. M. and Storey, K. B. (2009) Phosphorylation of translation factors in response to anoxia in turtles, Trachemys scripta elegans: role of the AMP-activated protein kinase and target of rapamycin signalling pathways. Molecular and cellular biochemistry. 332, 207-213
        48. Zhou, A. Y., Ichaso, N., Adamarek, A., Zila, V., Forstova, J., Dibb, N. J. and Dilworth, S. M. (2011) Polyomavirus middle T-antigen is a transmembrane protein that binds signalling proteins in discrete subcellular membrane sites. J Virol. 85, 3046-3054
        49. Rider, M. H., Hussain, N., Dilworth, S. M., Storey, J. M. and Storey, K. B. (2011) AMP-activated protein kinase and metabolic regulation in cold-hardy insects. J Insect Physiol. 57, 1453-1462
        50. Rahman, N. A., Bennink, H. J., Chrusciel, M., Sharp, V., Zimmerman, Y., Dina, R., Li, X., Ellonen, A., Rivero-Muller, A., Dilworth, S., Ghaem-Maghami, S., Vainio, O. and Huhtaniemi, I. (2012) A novel treatment strategy for ovarian cancer based on immunization against zona pellucida protein (ZP) 3. Faseb J. 26, 324-333.

        Refereed and published conference proceedings

        1. Griffin, B.E., Ito, Y., Novak, U., Spurr, N., Dilworth, S.M., Smolar, N., Pollack, R., Smith, K., and Rifkin, D.B.  (1980). Early Mutants of Polyoma Virus (dl8 and dl23) with Altered Transformation Properties: Is Middle T-Antigen a Transforming Gene Product? CSH Symposia on Quantitative Biology, 44 271-283.
        2. Griffin, B.E., Dilworth, S.M., Ito, Y., and Novak, U. (1980). Polyoma virus: some considerations on its transforming genes. Proc. R. Soc. Lond. B 210 465-476.
        3. Laskey, R.A., Dingwall, C., Mills, A.D., and Dilworth, S.M. (1985). Transport and Assembly of Nuclear Proteins. in Nuclear Envelope Structure and RNA Maturation. UCLA Symposia on Molecular and Cellular Biology, New Series 26 (Eds. Smuckler and Clawson). Liss Inc. New York. pp193-205.
        4. Laskey, R.A., Kearsey, S.E., Mechali, M., Dingwall, C., Mills, A.D., Dilworth, S.M., and Kleinschmidt, J. (1986). Chromosome replication in early Xenopus embryos. CSH Symposia on Quantitative Biology50 . 657-663
        5. Dingwall, C., Burglin, T.R., Kearsey, S.E., Dilworth, S.M., and Laskey, R.A. (1985).Sequence Features of the Nucleoplasmin Tail Region and Evidence for a Selective Entry Mechanism for Transport into the Cell Nucleus. Proc. of the Workshop on Nucleocytoplasmic Transport. (Eds. Peters and Trendelenburg) Heidelberg .
        6. Blow, J.J., Dilworth, S.M., Dingwall, C., Mills, A.D., and Laskey, R.A. (1987). Chromosome replication in Cell-free systems from Xenopus eggs. Phil. Trans. R. Soc. Lond. B. 317 483-494.
        7. Laskey, R.A., Mills, A.D., Philpott, A., Leno, G.H., Dilworth, S.M., and Dingwall, C. (1993). The Role of Nucleoplasmin in Chromatin Assembly and Disassembly. Philos. Trans. Roy. Soc. London. Biol. 339 263-269.

        Review Articles

        1. Dilworth, S.M., and Griffin, B.E. (1983). The transforming gene of polyoma virus. Arch. Geschwulstforsch. 53 187-195.
        2. Dilworth, S.M., and Dingwall, C. (1988). Chromatin Assembly In Vitro and In Vivo. Bioessays 9 44-49.
        3. Dilworth, S.M. (1990). Cell alterations induced by the large T-antigens of SV40 and polyoma virus. Seminar in Cancer Biology. 1 407-414.
        4. Dilworth, S.M. (1995). Polyoma virus middle T antigen: meddler or mimic? Trends in Microbiology. 3 31-35.
        5. Ichaso, N., and Dilworth, S.M. (2001). Cell transformation by the middle T-antigen of polyoma virus. Oncogene 20 7908-7916.
        6. Dilworth, S.M. (2002) Polyoma virus middle T antigen and its role in identifying cancer-related molecules. Nat. Rev. Cancer. 2 951-956.
        7. Dibb, N.J., Dilworth, S.M., and Mol, C.D. (2004). Switching on kinases: oncogenic activation of BRAF and the PDGFR family. Nat. Rev. Cancer. 4 718-727.
        8. Atkin, S.J., Griffin, B.E., and Dilworth, S.M. (2009). Polyoma virus and simian virus 40 as cancer models: history and perspectives. Semin Cancer Biol19, 211-217.

        Reviews in Books

        1. Griffin, B.E., and Dilworth, S.M. (1983). Polyoma virus: An Overview of its Unique Properties. Adv. Cancer Res. 39 183-268.
        2. Nicholson, P.R., and Dilworth, S.M. (2001). Polyoma virus middle T-antigen: growth factor receptor mimic. Editor Grand RJA. Title: Viruses, Cell Transformation and Cancer. Series Editors Zuckerman AJ, and Mushahwar I. Perspectives in Medical Virology Vol 5. Publisher Elsevier. pp85-128.

        Conference Proceedings

        Too many to list, but including presentations at most of the DNA Tumour Virus Meetings held every year, FEBS Meetings, including FEBS2009, Biochemical Society Meetings, BSCB/BSDB Meetings and Genes and Cancer Meetings.

        Publication Feed

        Modelling and validating three-dimensional human breast and cancerous human breast tissues in vitro

        Zuk, Anna Karolina and Burczynska, Beata and Li, Dong and Ghali, Lucy and Dilworth, Stephen M. and Wen, Xuesong (2020) Modelling and validating three-dimensional human breast and cancerous human breast tissues in vitro. Clinical Oncology and Research , 3 (4). pp. 1-9. ISSN 2613-4942

        Modelling and validating three dimensional human normal cervix and cervical cancer tissues in vitro

        Zuk, Anna Karolina and Wen, Xuesong and Dilworth, Stephen M. and Li, Dong and Ghali, Lucy (2017) Modelling and validating three dimensional human normal cervix and cervical cancer tissues in vitro. Journal of Biomedical Research , 31 (3). pp. 240-247. ISSN 1674-8301

        A novel treatment strategy for ovarian cancer based on immunization against zona pellucida protein (ZP) 3

        Rahman, Nafis A. and Bennink, Herjan J. T. C. and Chrusciel, Marcin and Sharp, Victoria and Zimmerman, Yvette and Dina, Roberto and Li, Xiangdong and Ellonen, Antti and Rivero-Müller, Adolfo and Dilworth, Stephen M. and Ghaem-Maghami, Sadaf and Vainio, Olli and Huhtaniemi, Ilpo (2012) A novel treatment strategy for ovarian cancer based on immunization against zona pellucida protein (ZP) 3. The FASEB Journal , 26 (1). pp. 324-333. ISSN 0892-6638

        AMP-activated protein kinase and metabolic regulation in cold-hardy insects

        Rider, Mark H. and Hussain, Nusrat and Dilworth, Stephen M. and Storey, Janet M. and Storey, Kenneth B. (2011) AMP-activated protein kinase and metabolic regulation in cold-hardy insects. Journal of Insect Physiology , 57 (11). pp. 1453-1462. ISSN 0022-1910

        Polyomavirus middle T-antigen is a transmembrane protein that binds signaling proteins in discrete subcellular membrane sites

        Zhou, Alice Y. and Ichaso, Natalia and Adamarek, Adam and Zila, Vojtech and Forstova, Jitka and Dibb, Nicholas J. and Dilworth, Stephen M. (2011) Polyomavirus middle T-antigen is a transmembrane protein that binds signaling proteins in discrete subcellular membrane sites. Journal of Virology , 85 (7). pp. 3046-3054. ISSN 0022-538X

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      • Funded Research &
        Knowledge Exchange Projects

        During my time at the RPMS and ICSM, over £2,000,000 in research grants has been raised. The group held two CRC Project Grants continuously for over 12 years, and has also received grants from the EC Biomed 2 Cancer Programme to study Protein Phosphatase 2A. The role of tyrosine phosphorylation sites in Shc signal transduction was funded by grants from the BBSRC, as was a proteomic project to identify and characterize novel MT binding proteins that is just producing results. In addition to this, we are collaborating with other CR UK Groups, particularly Prof. Laskey's, to develop clinically useful diagnostic monoclonal antibodies, and currently hold small awards from local funding schemes. Other grants have been gained in the past from the Royal Society, The Nuffield Foundation and the local SHA.

        Planned Grant Applications include one each to the CR UK and BBSRC to examine the way the hydrophobic domain of MT targets discrete signalling complexes in the membrane and an application to determine the other components of this signalling complex.

        YearOrganizationTitleAmount
        1999-2002 BBSRCSignalling Pathways activated by Shc phosphorylation £163,500
        1999-2003AICRThe membrane spanning domain in GFR signalling and MT£119,416
        2001-2006BELSPOTransmembrane transport and protein phosphorylation in the regulation of cell function£67,000
        2004-2007BBSRCSignal output by the adaptor protein Grb2: regulation by ShcA and phosphorylation.£178,000
        2004-2007BBSRCProteomic analysis of the novel proteins associated with the polyoma virus T-antigens and their role in cell function.£279,000
        2004-2010BBSRC Functional analysis of the nuclear receptor co repressor RIP140 Co-PI  £200,000
        2007-2011BELSPO Signal Integration Mechanisms in Health and Disease£66,000
        2008-2011IOG Trust Changes to the PP2A Interactome£18,000

      • Engagement &
        Impact

        Outside the University, I was a member of the North West Cancer Research Fund Scientific Committee for 7 years from 2001 to 2007.

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