Research Program: Carcinogenesis & Chemoprevention
Research Assistant Professor, Cellular and Molecular Biology Section, Hormel Institute, University of Minnesota

yongyeon@hi.umn.edu
507-437-9616 — office/lab phone
Preferred contact method: e-mail or phone

Biographical information

Dr. Cho received his M.S. from Chungnam National University, Korea, and Ph.D. from the Tohoku University, Japan, in the field of functional genomics. In December 2001, he came to the Hormel Institute's Cellular and Molecular Biology Section to conduct postdoctoral training in the laboratory of Dr. Zigang Dong. He is currently a research assistant professor.

Research Interests

My research focuses on researching new functions and/or new signaling pathways of proteins involving neoplastic cell transformation and cancer development by signaling networks, which can be directly applicable to designing new drugs and therapeutic methods. To achieve the goal of this research area, I will use protein-protein interaction by a mammalian two-hybridization system. In our experience, about 80-85 percent of proteins, which have binding activity in the mammalian two-hybrid system, were detected protein-binding by a immunoprecipatation experiment. Thus, the mammalian two-hybrid system is a very sensitive and valuable method to screen the protein-protein interaction in mammal cells.

We are interested in novel protein-protein interactions, which are involved in cell transformation and cancer development. In the cell, many proteins are linked physiologically depending on different environments. MAP kinase cascade is one of the most important signaling pathways to control the cell transformation, cell differentiation, cell proliferation, and/or cell death. When cells are stimulated with growth factors or other stresses, MAP kinases, especially ERKs, p38 kinases, and JNKs, are rapidly phosphorylated and transduce their signal to downstream kinases or transcription factors. Although signaling cascades of MAP kinases are relatively well understood compared with others, the exact signaling network of MAP kinases depending on different situations is not known. Therefore, our research projects are focusing on the role of MAP kinases signaling networks depending on the different stimuli or different situations involving in cell transformation as well as cancer development. Furthermore, we are interested in finding natural compound(s), which specifically inhibit MAP kinases as a target of chemopreventive agents.

Selected Publications

Ke Yao, Yong-Yeon Cho, H. Robert Bergen III, Benjamin J. Madden, Bu Young Choi, Wei-Ya Ma, Ann M. Bode, and Zigang Dong. NFAT3 is a negative regulator of Ras-JNK1/2-AP-1-induced cell transformation. Cancer Research, in press, 2007 (Co-first author).

Yong-Yeon Cho, Ke Yao, Ann M. Bode, H. Robert Bergen III, Benjamin J. Madden, Sang-Muk Oh, Svetlana Ermakova, Bong Seok Kang, Hong Seok Choi, Jung-Hyun Shim, and Zigang Dong. RSK2 mediates muscle cell differentiation through regulation of NFAT3. Journal of Biological Chemistry, 282(11): 8380-8392, 2007.

Chengrong Lu, Feng Zhu, Yong-Yeon Cho, Faqing Tang, Tatyana Zykova, Wei-Ya Ma, Ann M. Bode, and Zigang Dong. Cell Apoptosis: Requirement of H2AX in DNA ladder formation, but not for the activation of caspase-3. Molecular Cell, 23(1):121-132, 2006.

Bu Young Choi, Hong Seok Choi, Kwangseok Ko, Yong-Yeon Cho, Feng Zhu, Bong Seok Kang, Ermakova Svetlana P, Wei-Ya Ma, Ann M. Bode and Zigang Dong. The tumor suppressor, p16INK4a prevents cell transformation through inhibition of c-Jun phosphorylation and AP-1 activity. Nature Structure & Molecular Biology, 12(8):699-707, 2005.

Yong-Yeon Cho, Zhiwei He, Yiguo Zhang, Hong Seok Choi, Feng Zhu, Bu Young Choi, Bong Seok Kang, Wei-Ya Ma, Ann M. Bode and Zigang Dong. The p53 protein is a novel substrate of RSK2 and a critical intermediary for RSK2 and histone H3 interaction. Cancer Res., 65 (9):3596-3603, 2005.

Yong-Yeon Cho, Ann M. Bode, Hideya Mizuno, Bu Young Choi, Hong Seok Choi and Zigang Dong. A novel role for mixed-lineage kinase-like mitogen-activated protein triple kinase alpha in neoplastic cell transformation and tumor development. Cancer Res., 64(11):3855-3864, 2004.