Associate Professor in Oncology

608/262-8376  or 608/262-1989

6451 Wisconsin Institutes for Medical Research

Research Interests:Cell signaling pathways related to cancer; Structural biology; Biochemistry; Proteomics


My lab works on cell signaling that links to cancer, focusing on cell metabolism and genome integrity that are subjected to both environmental and cellular toxicity. Particularly, we are interested in the regulation networks of protein phosphatase 2A (PP2A), mTOR and PML nuclear body. Both PP2A and mTOR are key regulators of many essential cellular functions, including cell cycle progression, cell growth, proliferation and metabolism. They respond to broad cellular and environmental cues and are central targets of many environmental and cellular insults. For example, several viral proteins can hijack PP2A machinery and induce cellular transformation. Some tumor-inducing toxins primarily target PP2A and inhibit its phosphatase activity. 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. We use structural and proteomic approaches in combination with cell biology and biochemistry to elucidate the structure and function of the key components in the regulation of PP2A, Tor and PML, as well as the crosstalk among them.

  • Guo, F., Stanevich, V., Wlodarchak, N., Sengupta, R., Jiang, L., Satyshur, K. A., and Xing, Y.  Structural Basis of PP2A Activation by PTPA, an ATP-dependent Activation Chaperone.  Cell Res., 24(2):  190-203, 2014.
  • Guo, F., Wan, L., Zheng, A., Stanevich, V., Wei, Y., Satyshur, K. A., Shen, M., Lee, W., Kang, Y., and Xing, Y.  Structural Insights Into the Tumor-Promoting Function of the MTDH-SND1 Complex.  Cell Rep., 8(6):  1704-1713, 2014.
  • Kim, H., Guo, F., Brahma, S., Xing, Y ., and Burkard, M. E.  Centralspindlin Assembly and 2 Phosphorylations on MgcRacGAP by Polo-like Kinase 1 Initiate Ect2 Binding in Early Cytokinesis.  Cell Cycle, 13(18):  2952-2961, 2014.
  • Kotlo, K., Xing, Y., Lather, S., Grillon, J. M., Johnson, K., Skidgel, R. A., Solaro, R. J., and Danziger, R. S.  PR65A Phosphorylation Regulates PP2A Complex Signaling.  PLoS ONE, 9(1):e85000, 2014.
  • Stanevich, V., Zheng, A., Guo, F., Jiang, L., Wlodarchak, N., and Xing, Y.  Mechanisms of the Scaffold Subunit in Facilitating Protein Phosphatase 2A Methylation.  PLoS ONE, 9(1):e86955, 2014.
  • Wan, L., Lu, X., Yuan, S., Wei, Y., Guo, F., Shen, M., Yuan, M., Chakrabarti, R., Hua, Y., Smith, H. A., Blanco, M. A., Chekmareva, M., Wu, H., Bronson, R. T., Haffty, B. G., Xing, Y., and Kang, Y.  MTDH-SND1 Interaction Is Crucial for Expansion and Activity of Tumor-Initiating Cells in Diverse Oncogene- and Carcinogen-Induced Mammary Tumors. Cancer Cell, 26(1):  92-105, 2014.
  • Jiang, L., Stanevich, V., Satyshur, K. A., Kong, M., Watkins, G. R., Wadzinski, B. E., Sengupta, R., and Xing, Y.  Structural Basis of Protein Phosphatase 2A Stable Latency.  Nat. Commun., 4:1699, 2013.
  • Wlodarchak, N., Guo, F., Satyshur, K. A., Jiang, L., Jeffrey, P. D., Sun, T., Stanevich, V., Mumby, M. C., and Xing, Y.  Structure of the Ca2+-Dependent PP2A Heterotrimer and Insights into Cdc6 Dephosphorylation.  Cell Res., 23(7): 931-946, 2013.

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