Helen M. Piwnica-Worms, Ph.D. Professor Cell Biology and Physiology Internal Medicine Investigator Howard Hughes Medical Institute Molecular Cell Biology Program Biochemistry Program Molecular Genetics and Genomics Program
Office Phone: 314-362-6812 Lab Phone: 314-362-6834 Other Phone: FAX: 314-362-3709 Box: 8228 Lab Address: 554 McDonnell Medical Sciences Building Email: hpiwnica@cellbiology.wustl.edu Website: http://www.hhmi.org/research/investigators/piwnicaworms.html Keywords: breast cancer; cell cycle; DNA damage; functional genomics; imaging; signal transduction Short Research Description: Cell cycle and checkpoint control.
Research Abstract: The major goals of my research program are to delineate how the cell division cycle is regulated in unperturbed cycling cells (cell cycle control); how cell division is delayed by replicative- and genotoxic-stress (checkpoint control); how cancer cells derail these regulatory pathways and ultimately to use this information to treat human disease. Our current studies focus on (1) cell cycle control, with particular emphasis on the Cdc25 family of protein phosphatases; (2) checkpoint control, with emphasis on the Chk1 and Chk2 protein kinases; (3)establishment and maintenance of cell polarity with emphasis on the Par-1 polarity kinases (4) translational studies in the form of phase I clinical trials and a preclinical model of breast cancer and (5) applying methodologies to noninvasively image endogenous proteins in intact cells and in mice.
Selected Publications: Lee G, White LS, Hurov KE, et al. Response of small intestinal epithelial cells to acute disruption of cell division through Cdc25 deletion. Proc Natl Acad Sci USA 2008 24:4701-4706. Kang T, Wei Y, Honaker Y, et al. GSK-3beta targets Cdc25A for ubiquitin-mediated proteolysis, and GSK-3beta inactivation correlates with Cdc25A overproduction in human cancers. Cancer Cell 2008 13: 36-47. Lovly CM, Ling Y, Ryan CE, et al. Regulation of Chk2 ubiquitination and signaling through autophosphorylation of serine 379. Mol Cell Biol 2008 28:5874-5885. Watkins, JL, Lewandowski, KT, Meek, SEM, et al. Phosphorylation of Par-1 polarity kinase by protein kinase D regulates 14-3-3 binding and membrane association. Proc Natl Acad Sci USA 2008 105:18378-18383. Hurov JB, Huang M, White LS, et al. Loss of the Par-1b/MARK2 polarity kinase leads to increased metabolic rate, decreased adiposity, and insulin hypersensitivity in vivo. Proc Natl Acad Sci USA 2007 104: 5680-5685.

Last Updated: 10/27/2009