Assistant Professor of Oncology
B.S., 1995, Biochemistry, Fudan 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., Stock, J. B., Jeffrey, P. D., and Shi, Y. Structural Mechanism of Demethylation and Inactivation of Protein Phosphatase 2A. Cell, 133: 154-163, 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: 527-534, 2007.
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: 535-546, 2006.
Xing, Y., Xu, Y., Chen, Y., Jeffrey, P. D., Chao, Y., Lin, Z., Li, Z., Strack, S., Stock, J. B., and Shi, Y. Structure of Protein Phosphatase 2A Core Enzyme Bound to Tumor-Inducing Toxins. Cell, 127: 341-353, 2006. [The first three authors contributed equally to this work.]
Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., and Shi, Y. Structure of the Protein Phosphatase 2A Holoenzyme. Cell, 127: 1239-1251, 2006.
Bernard, M. P., Lin, W., Myers, R., Cao, D., Xing, Y., and Moyle, W. R. Crosslinked Bifunctional Gonadotropin Analogs with Reduced Efficacy. Mol. Cell. Endocrinol., 233: 25-31, 2005.
Bernard, M. P., Lin, W., Cao, D., Myers, R. V., Xing, Y., and Moyle, W. R. Only a Portion of the Small Seatbelt Loop in Human Choriogonadotropin Appears Capable of Contacting the Lutropin Receptor. J. Biol. Chem., 279: 44438-44441, 2004.
Moyle, W. R., Xing, Y., Lin, W., Cao, D., Myers, R. V., Kerrigan, J. E., and Bernard, M. P. Model of Glycoprotein Hormone Receptor Ligand Binding and Signaling. J. Biol. Chem., 279: 44442-44459, 2004.
Xing, Y., Lin, W., Jiang, M., Cao, D., Myers, R. V., Bernard, M. P., and Moyle, W. R. Use of Protein Knobs to Characterize the Position of Conserved α-Subunit Regions in Lutropin Receptor Complexes. J. Biol. Chem., 279: 44427-44437, 2004.
Xing, Y., Myers, R. V., Cao, D., Lin, W., Jiang, M., Bernard, M. P., and Moyle, W. R. Glycoprotein Hormone Assembly in the Endoplasmic Reticulum. I. The Glycosylated End of Human α-Subunit Loop 2 Is Threaded through a β-Subunit Hole. J. Biol. Chem., 279: 35426-35436, 2004.
Xing, Y., Myers, R. V., Cao, D., Lin, W., Jiang, M., Bernard, M. P., and Moyle, W. R. Glycoprotein Hormone Assembly in the Endoplasmic Reticulum. II. Multiple Roles of a Redox Sensitive β-Subunit Disulfide Switch. J. Biol. Chem., 279: 35437-35448, 2004.
Xing, Y., Myers, R. V., Cao, D., Lin, W., Jiang, M., 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. J. Biol. Chem., 279: 35449-35457, 2004.
Xing, Y., Myers, R. V., Cao, D., Lin, W., Jiang, M., 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: 35458-35468, 2004.
