The rockefeller university

Event Details

Type

Friday Lecture Series

Speaker(s)

Tony Hunter, Ph.D., Renato Dulbecco Chair in Cancer Research, American Cancer Society Professor, Molecular and Cell Biology Laboratory, director, Salk Institute Cancer Center, Salk Institute for Biological Studies

Speaker bio(s)

Post-translational modification (PTM) increases the complexity of the proteome, and reversible PTMs are used to transmit signals within cells in response to stimuli. Protein phosphorylation is involved in most cellular processes, and thousands of distinct phosphorylation events occur in a single cell type. The human kinome comprises more than 530 protein kinases (PKs); 480 are canonical eukaryotic PKs, and the remainder are atypical PKs; most are Ser/Thr kinases, but there are 90 Tyr kinases. In addition to Ser, Thr, and Tyr, six other amino acids can be phosphorylated, including histidine. Histidine phosphorylation may be a regulatory mechanism. To study global histidine phosphorylation events, Dr. Hunter’s laboratory generated monoclonal antibodies (mAbs) against noncleavable 1-pHis and 3-pHis analogues, and used them to study histidine phosphorylation. They used immobilized mAbs to affinity purify and identify ~800 proteins that putatively contain 1-pHis (~250) or 3-pHis (~160), from 293 cells, and have begun to characterize some of these. Anti–1-pHis mAbs stain the outside of phagocytic vesicles in primary macrophages and HeLa cells; immunostaining of proliferating HeLa cells with anti–3-pHis mAbs showed a striking pattern in mitotic cells, with strong signals for spindle poles (and centrosomes in interphase cells) and the midbody, suggesting that 3-histidine phosphorylation regulates the mitotic process.

 

In 1979, through his work on tumor viruses, Dr. Hunter discovered a new class of protein kinase that phosphorylates tyrosine. He has spent most of the last 35 years studying protein kinases and phosphatase, the role of protein phosphorylation in cell proliferation and the cell cycle, and how aberrant protein phosphorylation can cause cancer. Dr. Hunter’s laboratory also works on other types of PTMs, including ubiquitylation and sumoylation, and cross talk between PTMs.

 

Dr. Hunter received his Ph.D. from the University of Cambridge in 1969, where he was in Asher Korner’s laboratory. He was a research associate at the Salk Institute for Biological Studies from 1971 to 1973, returning as an assistant professor in 1975. He is currently the Renato Dulbecco Chair in Cancer Research and an American Cancer Society Professor in the Molecular and Cell Biology Laboratory at the Salk Institute. He is also director of the Salk Institute Cancer Center.

 

He is a member of the National Academy of Sciences and the National Academy of Medicine, and a fellow of The Royal Society, the American Academy of Arts and Sciences, and the American Association for Cancer Research Academy. Dr. Hunter has received several honors for his work, including the Canada Gairdner International Award in 1994, the American Cancer Society Medal of Honor in 2004, the Wolf Prize in Medicine in 2005, and the Lifetime Achievement in Cancer Research Award from the Jefferson Kimmel Cancer Center in 2011.

Open to

Public

Host

Sohail Tavazoie, M.D., Ph.D.

Reception

Refreshments, 3:15 p.m. - 3:45 p.m., Abby Lounge

Contact

Linda Hanssler

Phone

(212) 327-7714

Sponsor

Linda Hanssler
(212) 327-7714
lhanssler@rockefeller.edu

Readings

http://librarynews.rockefeller.edu/?p=4062