Dr. Stephanie Sen
B.A, (with honors) Bryn Mawr College
Ph.D. Stony Brook University
Post Doctoral Fellowship Research Institute of Scripps Clinic, Stanford University.
The objective of my research program is to determine the structure and function proteins that are involved in construction and regulation of isoprenoids, with particular emphasis on insect and plant metabolism.
Isoprenoids are a specialized group of natural products that are essential for a wide range of biochemical processes, including electron transport, sterol biosynthesis, and anchoring proteins to cellular membranes. In addition, they serve an important role in chemical communication (e.g., pheromones). It is fair to say that isoprenoids are not only ubiquitous in nature but structurally diverse, with over 50,000 distinct chemical structures known. While isoprenoids are produced and utilized by all organisms, the formation of more complex chemical structures is limited to certain species. In contrast to all other animals, insects synthesize a broad range of isoprenoid natural products that also occur in plants, making insect isoprenoid metabolism a hybrid between the animal and plant kingdoms.
Most of our current research has focused on insect isoprenoid metabolism. Specific projects include:
- Development of inhibitors of insect isoprenoid metabolism
- Characterization of type 1 farnesyl diphosphate synthase in moths
- Farnesol oxidation and its role in the construction of insect juvenile hormone
- Structure and function of isopentenyl diphosphate isomerase in insects
- Isopentenyl diphosphate transport in animals
Current group members
- Cusson, M., Sen, S.E., Shinoda, T. Juvenile Hormone Biosynthetic Enzymes as Targets for Insecticide Discovery.In Ishaaya, I., Palli, S.R., Horowitz, A.R., Eds., Advanced Technologies for Managing Insect Pests 2012, 31-55. Netherlands: Springer. http://link.springer.com/chapter/10.1007%2F978-94-007-4497-4_3#
- Sen. S.E., Tomasello, A., Grasso, M., Denton, R., Macor, J., Beliveau, C. Cusson, M., Crowell, D.N. Cloning, expression, and characterization of lepidopteran isopentenyl diphosphate isomerase. Insect Biochem. Mol. Biol. 2012, 42, 739-750. http://www.ncbi.nlm.nih.gov/pubmed/22820710
- Huizinga, D.H., Denton, R., Koehler, K.G., Tomasello, A., Wood, L., Sen, S.E.,* and Crowell, D.N.* Farnesylcysteine Lyase is Involved in Negative Regulation of Abscisic Acid Signaling in Arabidopsis. Mol Plant 2009, 3, 143-155. http://www.ncbi.nlm.nih.gov/pubmed/19969520
- Soni, S.P., Ward, J.A., Sen, S.E., Feller, S.E., and Wassall,* S.R. Effect of Trans Unsaturation on Molecular Organization in a Phospholipid Membrane. Biochemistry 2009, 48, 11097-11107. http://pubs.acs.org/doi/abs/10.1021/bi901179r
- Henry, O., Lopez-Gallego, F., Agger, S.A., Schmidt-Dannert, C., Sen, S., Shintani, D., Cornish, K., and Distefano, M.D.* A versatile photoactivatable probe designed to label the diphosphate binding site of farnesyl diphosphate utilizing enzymes. Bioorg. Med. Chem. 2009, 17, 4797-4805. http://www.ncbi.nlm.nih.gov/pubmed/19447628