Anthony Pawson

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Professor
Anthony Pawson
OC OOnt CH FRS FRSC PhD MA
Born (1952-10-18) October 18, 1952 (age 60)
Maidstone, England
Nationality  United Kingdom
 Canada
Fields Genetics, microbiology
Institutions University of Toronto
Mount Sinai Hospital, Toronto
Samuel Lunenfeld Research Institute
Alma mater University of Cambridge
King's College London
Known for Cellular signal transduction
Notable awards Wolf Prize in Medicine (2005)

Anthony 'Tony' James Pawson, OC OOnt CH FRS FRSC (born October 18, 1952), British-born Canadian scientist whose research has revolutionized the understanding of signal transduction, the molecular mechanisms by which cells respond to external cues, and how they communicate with each other. He identified the phosphotyrosine-binding Src homology 2 (SH2 domain) as the prototypic non-catalytic interaction module. SH2 domains serve as a model for a large family of protein modules that act together to control many aspects of cellular signaling. Since the discovery of SH2 domains, hundreds of different modules have been identified in many proteins.

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Biography[edit]

Born in Maidstone, England, the son of the cricketer and writer Tony Pawson, he was educated at Winchester College and the University of Cambridge where he received a MA in biochemistry followed by a Ph.D. from King's College London in 1976. From 1976 to 1980 he pursued postdoctoral work at the University of California, Berkeley. From 1981 to 1985, he was Assistant Professor at the University of British Columbia.

Dr. Pawson is a Distinguished Investigator and former Director of Research at the Samuel Lunenfeld Research Institute of Mount Sinai Hospital and Professor in the Department of Molecular Genetics at the University of Toronto both of which he joined in 1985.

Honours and awards[edit]

Selected publications[edit]

  • Pawson, T. & Nash, P. (2003) Assembly of cell regulatory systems through protein interaction domains. Science 300: 445-452. [1]
  • Nash, P., Tang, X., Orlicky, S., Chen, Q., Gertler, F.B., Mendenhall, M.D., Sicheri, F., Pawson, T., Tyers, M. (2001) Multi-site phosphorylation of a CDK inhibitor sets a threshold for the onset of DNA replication. Nature 414: 514-521. [2]
  • Holland, S. J., Gale, N. W., Mbamalu, G., Yancopoulos, G. D., Henkemeyer, M., & Pawson, T. (1996). Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands. Nature 383(6602), 722-5. (Link to article)
  • Salcini, A. E., McGlade, J., Pelicci, G., Nicoletti, I., Pawson, T., & Pelicci, P. G. (1994). Formation of Shc-Grb2 complexes is necessary to induce neoplastic transformation by overexpression of Shc proteins. Oncogene, 9(10), 2827-36. (Link to article)
  • Henkemeyer, M., Marengere, L. E., McGlade, J., Olivier, J. P., Conlon, R. A., Holmyard, D. P., Letwin, K., & Pawson, T. (1994). Immunolocalization of the Nuk receptor tyrosine kinase suggests roles in segmental patterning of the brain and axonogenesis. Oncogene, 9(4), 1001-14. (Link to article)
  • Stephens, R. M., Loeb, D. M., Copeland, T. D., Pawson, T., Greene, L. A., & Kaplan, D. R. (1994). Trk receptors use redundant signal transduction pathways involving SHC and PLC-gamma 1 to mediate NGF. Neuron, 12(3), 691-705. (Link to article)
  • Crowe, A. J., McGlade, J., Pawson, T., & Hayman, M. J. (1994). Phosphorylation of the SHC proteins on tyrosine correlates with the transformation of fibroblasts and erythroblasts by the v-sea tyrosine kinase. Oncogene, 9(2), 537-44. (Link to article)
  • Marengere, L. E., Zhou, S., Gish, G. D., Schaller, M. D., Parsons, J. T., Stern, M. J. Cantley, L. C., & Pawson, T. (1994). SH2 domain specificity and activity modified by a single residue. Nature, 369(6480), 502-5. (Link to article)

References[edit]

External links[edit]