Gokul Das

PhD

Cancers Treated:

Special Interests:

Interaction between estrogen receptors and tumor suppressor protein p53 signaling in breast cancer: understanding molecular mechanisms and identifying new prognostic markers and therapeutic targets Role of p53 and estrogen receptor beta in non-small cell lung cancer (NSCLC) pathology Cellular and molecular underpinnings of the role of estrogen receptors and mutant p53 in high grade serous ovarian cancer (HGSOC) Estrogen receptors and p53 in the regulation of nuclear-mitochondrial communication and energy metabolism Clinical trials to translate research findings from the laboratory

About Gokul Das

Positions

Roswell Park Comprehensive Cancer Center

  • Professor of Oncology
  • Department of Pharmacology & Therapeutics
  • Member, Experimental Therapeutics Graduate Program, Cancer Sciences Track
  • Member, Developmental Therapeutics CCSG Program
  • Co-Director, Breast Translational Research Group (TRG)
  • Member, Lung TRG
  • Member, Gynecology TRG

Background

Education and Training:

  • PhD - Pharmacology & Molecular Biology - Baylor College of Medicine, Houston, Texas

Fellowship:

  • Post-doctoral: Cold Spring Harbor Laboratory, Cold Spring Harbor, NY

Professional Memberships:

  • American Association for Cancer Research (AACR)
  • The American Society of Pharmacology and Experimental Therapeutics (ASPET)

Research

Research Overview:

Research in my laboratory focuses on crosstalk between estrogen receptors and p53 signaling in breast, lung, and ovarian cancers. Inactivation of p53 by multiple mechanisms is a frequent event in these cancers. Estrogen receptors alpha (ERα) and beta (ERβ) have important roles in normal and disease physiology of these organs. We have shown that both ERα and ERβ bind p53. Binding of ERα to p53 results in functional inactivation of p53, whereas ERβ-p53 interaction elicits context-dependent effects in cancer cells.


Publications

Full Publications list on PubMed

Key Publications

  • • Oturkar, CC., Gandhi, N., Rao, P., Eng, KH., Miller, A., Singh, PK., Zsiros, E., Odunsi, KE., and Das, G.M. (2021). Estrogen receptor-beta2 (ERβ2)-mutant p53-FOXM1 axis is an important driver of proliferation, chemoresistance, and disease progression in high grade serous ovarian cancer (HGSOC). Cancers, 14: 1120, https://doi.org/10.3390/ cancers14051120
    • Mukhopadhyay, UK., Otukar, C., Adams, C., Wickramasekera, N., Bansal, S., Medisetty, R., Miller, A., Swetzig, WM., Silwal-Pandit, L., Borresen-Dale, Al., Creighton, C.J., Oturkar,C., Konduri, SD., Mukhopadhyay, A., Omilian, A., Bshara, W., Kaipparettu, BA., Das, GM. (2019). TP53 status as a determinant of pro- versus anti-tumorigenic effects of estrogen receptor-beta in breast cancer. Journal of the National Cancer Institute (JNCI), 111 (11):1202-1215. djz051.
    • Putluri, P., Maity, M., Kommangani, R., Creighton, C. J., Putluri, V., Chen, F., Nanda, S., Bhowmik, S. K., Terunuma, A., Dorsey, T., Nardone, M., Fu, X., Shaw, C., Sarkar, T.R., Schiff, R., Lydon, J. P., O’Malley, B.W., Ambs,S., Das, G. M., Michailidis, G., and Sreekumar, A. (2014). Pathway-centric integrative analysis identifies RRM2 as a prognostic marker in breast cancer associated with poor survival and tamoxifen resistance. Neoplasia, 16, 330-402
    • Konduri, S., Medisetty, R., Liu, W., Kaipparettu, B., Srivastava, P., Brauch, H., Fritz, P., Swetzig, W., Gardner, A., Khan, S. & Das, G.M.(2010). Mechanisms of Estrogen receptor antagonism towards p53 and its implications in breast cancer therapeutic response and stem cell regulation. Proc Natl Acad Sci, USA (PNAS), 107, 15081-15086. PMCID: PMC2930589.
    • Sayeed, A., Konduri, S., Liu, W., Bansal, S., Li, F. & Das, G.M. (2007). Estrogen receptor inhibits p53-mediated transcriptional repression: Implications for the regulation of apoptosis. Cancer Research; 67, 7746-7755, PMID: 17699779.
    • Liu, W., Konduri, S., Bansal, S., Nayak, B.K., Rajasekaran, S.A., Karuppayil, S.M., Rajasekaran, A.K. & Das, G.M. (2006). Estrogen receptor-α binds p53 tumor suppressor protein directly and represses its function, Accelerated Report, J Biological Chemistry; 281, 9837-9840, PMID: 16469747