Tony Hunter

Salk Institute for Biological Studies


Primary Section: 41, Medical Genetics, Hematology, and Oncology
Secondary Section: 21, Biochemistry
Membership Type:
Member (elected 1998)

Biosketch

Tony Hunter received his BA and PhD from the University of Cambridge, England, and completed postdoctoral training at the Salk Institute for Biological Studies and the University of Cambridge. He joined the faculty of the Salk Institute in 1975, where he is currently Professor and Renato Dulbecco Chair in Cancer Research. In 1979, through his work on tumor viruses, he discovered a new class of protein kinases that phosphorylates tyrosine residues in proteins, establishing that dysregulated tyrosine phosphorylation by an activated tyrosine kinase can cause cancer.  He and others went on to show that tyrosine phosphorylation is a widespread reversible protein modification essential for the regulation of a wide variety of cellular processes in multicellular eukaryotes, including transmembrane signal transduction by surface receptors.  His work led to the realization that aberrant tyrosine phosphorylation is causal in several types of human cancer and in other diseases, and this has led to the successful development of small molecule inhibitors that target disease-causing tyrosine kinases, known as TKIs, such as Gleevec, a BCR-ABL inhibitor used for treatment of chronic myelogenous leukemia.  Hunter has received many awards for his work on tyrosine phosphorylation.

Research Interests

The Hunter group's main focus is on the role of protein phosphorylation in regulating cellular signaling events, and how aberrant phosphorylation causes cancer. His group also works on other types of post-translational modifcations (PTMs), including ubiquitylation, where he discovered the RING domain class of E3 Ub ligases, and sumoylation, where he identified a class of E3 ubiquitin ligases, STUbLs, that specifically target sumoylated proteins for ubiquitylation. For the past few years, he has been studying histidine phosphorylation of proteins, and has generated monoclonal antibodies specific for the two isoforms of phosphohistidine, which he used to identify many new histidine phosphorylated proteins, and to uncover a possible role for histidine phosphorylation in liver cancer. Most recently, he has investigated the role of stromal cells in pancreatic cancer, discovering a role for the leukemia inhibitory factor (LIF) cytokine secreted by cancer-associated fibroblasts in tumor progression.

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