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| Name |
Hunter, Tony |
| Location
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Salk Institute for Biological Studies |
| Primary Field
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Medical Genetics, Hematology and Oncology |
| Secondary Field
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Biochemistry |
 Election Citation
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Hunter is a biochemist from the United Kingdom. He was the first to identify phosphotyrosine protein modifications and the prototypic tyrosine protein kinase. This work stimulated all of the many subsequent studies that have elucidated the fundamental role of these protein kinases in cellular signal transduction, growth control, and morphogenesis.
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Research Interests
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For the past 25 years I have been studying the role of protein phosphorylation and dephosphorylation in cell growth and signal transduction. This interest started when I discovered that the transforming proteins of two animal tumor viruses have associated protein kinase activities that specifically phosphorylate tyrosine residues in proteins. Subsequently, many different protein-tyrosine kinases have been found, and we now know that the human genome has 90 tyrosine kinase genes. Tyrosine kinases are involved in a wide variety of processes, including growth control, cell cycle control, differentiation, cell shape and movement, transcription, synaptic transmission, and insulin action. In particular, tyrosine phosphorylation is widely used as a means of transducing signals across the cell membrane upon the binding of ligands to surface receptors. Aberrant tyrosine phosphorylation is involved in many types of disease, and over half of the 90 human tyrosine kinases have been implicated in cancer either as a result of overexpression or mutations that upregulate their activity. Following the discovery of tyrosine phosphorylation, I have focused on finding out how tyrosine phosphorylation triggered by surface receptors stimulates cell growth and how perturbations in normal tyrosine phosphorylation cause cancer. My main current interests are how tyrosine and serine/threonine kinases transduce signals inside the cell in response to activation of surface receptors. We also study the protein-tyrosine phosphatases that remove the phosphates added by tyrosine kinases. I also have an interest in how phosphorylation by cyclin-dependent protein kinases and other cell cycle protein kinases regulates ordered progression through the cell cycle, and activates cell cycle checkpoints in response to DNA or spindle damage both in fission yeast and mammalian cells. Finally, we work on the structure and function of ubiquitin ligases, and how protein ubiquitination and sumoylation is used to regulate signal transduction pathways and cell cycle progression.
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