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PULSe Home > Faculty Members A-C > Harry Charbonneau
Harry Charbonneau
Current Research Interests:
Protein phosphorylation is a major mechanism for ensuring the order and timing of the complex sequence of events required for a eukaryotic cell to divide. We are interested in the role of protein phosphatases in controlling essential transitions that occur during cell division. Our studies focus on the Cdc14 phosphatase, which triggers events necessary for cells to terminate mitosis and begin a new round of cell division. We use biochemical and molecular genetic approaches in the budding yeast system to delineate the diverse functions of Cdc14 during late mitosis and to define the regulatory mechanisms that modulate its activity. In complementary projects, we are also studying the mitotic functions and regulation of two distinct human Cdc14 phosphatases. Understanding the role of phosphorylation in cell proliferation is important because defects in coordinating the multiple cellular processes required for cell division are involved in the development of cancer.
Selected Publications:
Wang, W. Q., Bembenek, J., Gee, K. R, Yu, H., Charbonneau, H. and Zhang, Z. Y. (2004) Kinetic and mechanistic studies of a cell cycle protein phosphatase Cdc14. J. Biol. Chem. 279:30459-30468.
Traverso, E. E., Baskerville, C., Liu, Y., Shou, W., James, P., Deshaies, R., J., and Charbonneau, H. (2001) Characterization of the Net1 Cell Cycle-dependent Regulator of the Cdc14 Phosphatase from Budding Yeast. J. Biol. Chem. 276:21924-21931.
Shou, W., Sakamoto, K.. M., Keener, J., Morimoto, K. W., Traverso, E. E., Azzam, R., Hoppe, G. J., Feldman, R. R. M., DeModena, J., Moazed, D., Charbonneau, H., Nomura, M., and Deshaies, R. J. (2001) Net1 stimulates RNA Polymerase I transcription and regulates nucleolar structure independently of controlling mitotic exit. Mol. Cell 8:45-55.
Shou, W., J.H. Seol, A. Shevchenko, C. Baskerville, D. Moazed, Z.W.S. Chen, J. Jang, A. Shevchenko, H. Charbonneau, and R.J. Deshaies. (1999) Exit from mitosis is triggered by Tem1-dependent release of the protein phosphatase Cdc14 from the nucleolar RENT complex. Cell. 97:233-244.
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