2008 Kyoto Prize Laureates

Basic Sciences

Life Sciences and Medicine(Molecular Biology, Cell Biology, Systems Biology, etc.)

Anthony James Pawson

/  Molecular Biologist

1952 - 2013

Distinguished Investigator, Samuel Lunenfeld Research Institute of Mount Sinai Hospital ; University Professor, University of Toronto

Commemorative Lectures

Thinking about How Living Things Work


11 /11 Tue

Place:Kyoto International Conference Center


Signal Network in Biological Functions


11 /12 Wed

13:00 - 17:00

Place:Kyoto International Conference Center

Achievement Digest

Proposing and Proving the Concept of Adapter Molecules in the Signal Transduction

Dr. Pawson proposed and proved the concept that the unique adapter structure exists in signaling proteins, and that the binding of adapters to specific phosphotyrosine-containing domains induces cascades of intracellular signaling that controls cellular growth and differentiation. This concept has established one of the basic paradigms of signal transduction and significantly contributed to the subsequent development in life sciences.

*This field then was Field of Life Sciences (Molecular Biology, Cell Biology, Neurobiology).


Dr. Anthony James Pawson discovered a new mechanism of intracellular signal transduction, revealing an important molecular infrastructure that controls cellular growth and differentiation. In the late 1970s, the autophosphorylation of oncogene products and growth factor receptors was found at specific tyrosine residues, but the molecular mechanism of signal transduction beyond tyrosine phosphorylation remained unknown. Dr. Pawson demonstrated that intracellular signaling proteins carry a domain with a unique modular structure, which he termed Src homology 2 (SH2), and that this domain recognizes and binds the phosphotyrosine and the flanking amino acids of target molecules to induce cascades of intracellular signaling that facilitates cellular growth and differentiation.

Based on his finding that not only the catalytic domains (tyrosine kinases) but also the flanking domains in oncogene products are necessary for the transformation (i.e., cancer-like behavior) of cells, Dr. Pawson discovered that oncogene products and signaling proteins share a common sequence consisting of approximately 100 amino acid residues, which he termed SH2, and that the SH2 domain takes part in the interaction between tyrosine kinases and their substrates. He proposed that SH2 domains act as adapters that mediate the binding with cell membrane receptors and cytoskeletal proteins, by showing for the first time that there is a protein that can bind to the phosphotyrosine of a signaling protein, RasGAP. He disclosed that various SH2 domains can directly bind tyrosine-phosphorylated proteins in vitro. Furthermore, he demonstrated that the binding strength between SH2 domains and their target proteins varies, explaining that each SH2 domain binds to a specific tyrosine-phosphorylated protein to induce specific intracellular signaling cascades.

These achievements by Dr. Pawson laid out the scheme that adapter molecules facilitate successive protein-protein associations like the Lego blocks, thereby participating in the fundamental mechanism of signal transduction that controls cellular growth and differentiation, as well as development of cancer. Consequently, the proposal and proof of the concept for adapter molecules by Dr. Pawson have established one of the basic paradigms in signal transduction and contributed significantly to the subsequent development in life sciences.

For these reasons, the Inamori Foundation is pleased to present the 2008 Kyoto Prize in Basic Sciences to Dr. Anthony James Pawson.


Born in Maidstone, U.K.
Ph.D. (Molecular Biology), London University
Postdoctoral Research Fellow, University of California, Berkeley
Assistant Professor, Department of Microbiology, The University of British Columbia
Senior Investigator, Samuel Lunenfeld Research Institute, Mount Sinai Hospital
Associate Professor, Department of Medical Genetics and Microbiology, University of Toronto
Full Professor, Department of Medical Genetics and Microbiology (now Department of Molecular Genetics), University of Toronto
University Professor, University of Toronto
Director of Research, Samuel Lunenfeld Research Institute, Mount Sinai Hospital
Distinguished Investigator, Samuel Lunenfeld Research Institute, Mount Sinai Hospital
Selected Awards and Honors
International Award, Gairdner Foundation
Officer of the Order of Canada
Wolf Foundation Prize in Medicine, Wolf Foundation
The Royal Medal, Royal Society of London
Order of the Companions of Honour
Royal Society of London, Royal Society of Canada, National Academy of Sciences, American Academy of Arts and Sciences
Selected Publications
Identification of functional regions in the transforming protein of Fujinami sarcoma virus by in-phase insertion mutagenesis (Stone, J. C., Atkinson, T., Smith, M. E. and Pawson, T.). Cell 37: 549-558, 1984.
A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps (Sadowski, I., Stone, J. C. and Pawson, T.). Molecular Cellular Biology 6: 4396-4408, 1986.
Binding of SH2 domains of phospholipase Cγ1, GAP and Src to activated growth factor receptors (Anderson, D., Koch, C. A., Grey, L., Ellis, C., Moran, M. F. and Pawson, T.). Science 250: 979-982, 1990.
Src homology region 2 domains direct protein-protein interactions in signal transduction (Moran, M., Koch, C. A., Anderson, D., Ellis, L., England, L., Martin, G. S. and Pawson, T.). Proceeding National Academy of Sciences, U.S.A. 87: 8622-8626, 1990.

Profile is at the time of the award.

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