Eileen J. Kennedy, Ph.D.
Pharmaceutical and Biomedical Sciences
|Ph.D. Chemistry (Biochemistry)||University of California, San Diego||La Jolla||2005|
|M.S. Chemistry (Biochemistry)||University of California, San Diego||La Jolla||2002|
|B.S. Biochemistry||University of Washington||Seattle||1998|
- Post-doctoral Experience
- Research Associate, Chemistry and Chemical Biology, Harvard University, Cambridge, MA July 2009-June 2010
Postdoctoral Fellow, Chemistry and Chemical Biology, Harvard University, Cambridge, MA January 2006-June 2009
- Honors and Awards
- 2011 Minority Young Scientist Travel Award by ASBMB/ASPET for Experimental Biology
2009 Scholar-in-Training Award, AACR-ACS Joint Conference for Chemistry in Cancer Research
2008 Burroughs Wellcome Fund’s Career Awards at the Scientific Interface, National Finalist
2007 Scholar-in-Training Award, AACR-ACS Joint Conference for Chemistry in Cancer Research
2006-2009 American Cancer Society Postdoctoral Fellow
2003-2005 American Heart Association Predoctoral Fellow
- Research Interests
- The protein kinase superfamily comprises one of the largest gene families encoded in the human genome. A comprehensive understanding of kinase activity under normal and disease states is critical in order to identify targets for disease intervention. However, studying kinase signaling is inherently challenging since there are over 500 kinases in the human genome, and as a result, there is significant crosstalk among multiple kinases for phosphorylation targets. Additionally, multiple isoforms exist for many kinases, thereby making it nearly impossible to address the question using genetic knockdowns/knockouts since other genes will compensate with altered expression levels. To address this question, Dr. Kennedy's lab is developing novel chemical biology strategies to synthetically disrupt protein:protein interactions (PPIs) using chemically stabilized peptides. This methodology allows them to develop investigative tools that can be applied to elegantly and selectively manipulate protein-protein interactions that are involved in signaling pathways within a cellular environment. Their long-term goal is to develop synthetic biologics that can be used to probe cell signaling events that are mediated by kinases. By inhibiting specific protein-protein interactions within a cellular environment, cancer-related cell signaling events can be studied in a temporal manner and highlight new strategies for therapeutic intervention. They are applying this strategy to study the AGC family of kinases as well as EGFR in breast and lung cancer models.
- Representative Publications
- Kennedy, E. J., Yang, J., Pillus, L., Taylor, S. S., and Ghosh, G. (2009) “Identifying critical non-catalytic residues that modulate PKA activity.” PLoS One, 4:e4746, (PMCID 19270744).
Yang, J., Kennedy, E. J., Wu, J., Deal, M. S., Pennypacker, J., Ghosh, G., and Taylor, S. S. (2009) “Contribution of non-catalytic core residues to activity and regulation in PKA.” J. Biol. Chem., 284: 6241-6248, (PMCID 19122195).
Kennedy, E. J., Ghosh, G., and Pillus, L. (2008) “Identification of functionally distinct regions that mediate biological activity of the Protein Kinase A homolog Tpk2.” J. Biol. Chem., 283: 1084-1093, (PMCID 17971450).
Kennedy, E. J., Pillus, L., and Ghosh, G. (2005) “Pho5p and newly identified E-NPPs regulate nucleotide phosphate metabolism in S. cerevisiae,” Eukaryotic Cell, 11: 1892-1901, (PMCID 16278456).