Bin-Tao Pan, Ph. D.
Room 310, Combs Building
University of Kentucky
800 Rose Street
Lexington, KY 40536
• Graduate Center for Nutritional Sciences
• Department of Surgery
• Department of Microbiology, Immunology, and Molecular Genetics
• Lucille P. Markey Cancer Center
• B.S., National Taiwan University, Taiwan
• Ph.D., McGill University, Canada
• Postdoctoral Fellow, Harvard Medical School
• Leukemia Society of America, postdoctoral fellowship
• NIH, postdoctoral fellowship
Specific Interest in Nutrition:
Role of nutrients in cancer development
Nutrients play an important role in the development of cancers. My laboratory is interested in studying the role of nutrients such as amino acids in the development of cancer. Amino acids are not only substrates for protein synthesis. Amino acids are also modulators for the signaling pathways involved in the regulation of protein synthesis and degradation. A pathway regulated by amino acids, especially leucine, involves the phosphorylation of ribosomal protein S6, which has been implicated in the regulation of protein synthesis and degradation. Interestingly, oncogenic Ras, the most common oncogenic protein detected in cancers, also induces S6 phosphorylation. It indicates that amino acids and oncogenic Ras share overlapped pathway(s) in the regulation of protein synthesis and degradation, further suggesting the possibility that nutrients such as leucine may contribute to cancer development through the overlapped pathway(s). We are currently studying the interplay between nutrients and oncogenic Ras in the regulation of protein synthesis and degradation, with a focus on the effect on the cell cycle.
Selected Recent Publications
Chen, D.H., Chen, C.T., Zhang, Y., Liu, M.A., Campos-Gonzalez, R., and Pan, B.T. Characterization of p96: immunoreaction with an anti-Erk peptide antibody and activity in Xenopus oocytes and eggs. Biochem. J. 335:43-50, 1998.
Pan, B.-T., Zhang, Y., Brott, B., and D.-H. Chen. The 96kDa protein kinase activated by oncogenic Ras in Xenopus egg extracts is also activated by constitutively active Mek: activation requires serine/threonine phosphorylation. Oncogene 14, 1653-1660, 1997.