Assistant Professor of Oncology
B.S., 1995, Biochemistry, Fudan University University, China
M.S., 1997, Institute of Genetics, Fudan University, China
Ph.D., 2002, Molecular Biology, Rutgers
University and UMDNJ, Piscataway, NJ.
Postdoctoral research: Princeton University, Princeton, NJ.
Office: 525A McArdle Laboratory
Telephone: Office – (608) 262-8376;
Lab – (608) 262-1989
Email: xing@oncology.wisc.edu
Research Interests: Cell signaling pathways related to cancer; Structural biology; Biochemistry; Proteomics
Research Description: My lab is interested in elucidation of signaling pathways related to cancer using multi-disciplinary biophysics and biochemical approaches, including structural biology and proteomics, in combination with cell biology. We focus on signaling pathways that affect cancer cell metabolism and cancer cell genome integrity.
Protein phosphatase 2A (PP2A) is involved in many essential cellular functions. Deregulation of PP2A function is frequently linked to multiple types of cancer. The importance of PP2A function also resides in its crosstalk with the Tor signaling pathway, which has broad effects on cell growth and metabolism. PP2A also interacts with PML, a major component of PML-nuclear body (PML-NB) that is missing in later stage of tumors. PML is considered an important tumor suppressor and has important functions in genome integrity and as an antiviral. Structural biology in combination with biochemistry and proteomics will provide powerful tools for elucidation of the structure and function of the key components in the regulation of PP2A, Tor and PML, as well as the crosstalk among them. Results from these aspects of our research will have a direct impact on the design of therapeutics against cancer.
Selected Recent Publications:
Xing Y, Li, Z., Chen, Y., Jeffrey, P.D., Stock, J.B., and Shi, Y. Structural mechanism of PP2A demethylation and inactivation. Cell, in press, 2008.
Chen, Y., Xu, Y, Bao Q, Xing, Y., Li, Z., Lin Z, Stock, J.B., Jeffrey, P.D., and Shi, Y. Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40. Nat Struct Mol Biol, 14: 527-34, 2007.
Xing, Y., Xu, Y., Chen, Y., Jeffrey, P.D., Chao, Y., Lin, Z., Li, Z., Stock, J.B., and Shi, Y. Structure of the Protein Phosphatase 2A Core Enzyme Bound to Tumor-inducing Toxins. Cell, 127: 341-53, 2006.
Xu, Y., Xing, Y., Chen, Y., Chao, Y., Jeffrey, P.D., Lin, Z., Li, Z., Stock, J.B., and Shi, Y. Structure of the Protein Phosphatase 2A holoenzyme bound to B’γ1. Cell, 127: 1239-1251, 2006.
Chao, Y., Xing, Y., Chen, Y., Xu, Y., Lin, Z., Li, Z., Jeffrey, P.D., Stock, J.B., and Shi, Y., Structure and mechanism of the phosphotyrosyl phosphatase activator. Mol Cell, 23: 535-46, 2006.
Bernard MP, Lin W, Myers R, Cao D, Xing Y, Moyle WR. Crosslinked bifunctional gonadotropin analogs with reduced efficacy. Mol Cell Endocrinol., 233: 25-31, 2005.
Xing Y, Lin W, Jiang M, Cao D, Myers RV, Bernard MP, Moyle WR. Use of protein knobs to characterize the position of conserved alpha-subunit regions in lutropin receptor complexes. J Biol Chem., 279: 44427-37, 2004.
Bernard MP, Lin W, Cao D, Myers RV, Xing Y, Moyle WR. Only a portion of the small seatbelt loop in human choriogonadotropin appears capable of contacting the lutropin receptor. J Biol Chem., 279: 44438-41, 2004.
Moyle WR, Xing Y, Lin W, Cao D, Myers RV, Kerrigan JE, Bernard MP. Model of glycoprotein hormone receptor ligand binding and signaling. J Biol Chem., 279: 44442-59, 2004.
Xing Y, Lin, W., Jiang, M., Cao, D., Myers, R.V., Bernard, M.P., and Moyle, W.R. Glycoprotein Hormone Assembly In The Endoplasmic Reticulum I: The Glycosylated End Of Human α-Subunit Loop Two Is Threaded Through A β-Subunit Hole. J Biol Chem., 279: 35426-36, 2004.
Xing Y, Lin, W., Jiang, M., Cao, D., Myers, R.V., Bernard, M.P., and Moyle, W.R. Glycoprotein Hormone Assembly In The Endoplasmic Reticulum II: Multiple Roles Of A Redox Sensitive β-SubunitDisulfide Switch. J Biol Chem., 279: 35437-48, 2004.
Xing Y, Lin, W., Jiang, M., Cao, D., Myers, R.V., Bernard, M.P., and Moyle, W.R. Glycoprotein Hormone Assembly In The Endoplasmic Reticulum III: The Seatbelt And Its Latch Site Determine The Assembly Pathway. Multiple Roles Of A Redox Sensitive β-Subunit Disulfide Switch. J Biol Chem., 279: 35449-57, 2004.
Xing Y, Lin, W., Jiang, M., Cao, D., Myers, R.V., Bernard, M.P., and Moyle, W.R. Glycoprotein Hormone Assembly In The Endoplasmic Reticulum IV: Probable Mechanism Of Subunit Docking And Completion Of Assembly. J Biol Chem., 279: 35458-68, 2004.
