More About The Gabriela Chiosis Lab Minus iconIcon indicating subtraction, or that the element can be closed. Plus IconIcon indicating addition, or that the element can be opened. Arrow (down) icon.An arrow icon, usually indicating that the containing element can be opened and closed.

Chao Xu, PhD

Research Fellow

Start Year

2014

 

I received my PhD in biochemistry and biophysics from the Institute of Biophysics, Chinese Academy of Sciences. Then I worked as postdoc fellow in Roswell Park Cancer Institute where I studied the regulation of Mdm2 ubiquitination and the p53 response by NEDD4-1 E3 ligase.

In 2014, I joined Chiosis lab at Memorial Sloan Kettering Cancer Center. In Chiosis lab, I am interested in understanding the mechanisms of Heat Shock Protein 70 (HSP70) in cancer. Heat shock protein 70 family members (HSP70s) are important cancer chaperone proteins. Through using the HSP70 chemical tools, we identified and analyzed the HSP70 interactome in cancer and investigated the HSP70 regulated mechanisms of anti-apoptosis and cell cycle control. In Chiosis lab, I am actively involved in a multi-disciplinary research team. That includes collaboration with chemists to study the PK & PD effects of novel HSP70 inhibitors and collaboration with physician to evaluate the potency of HSP70 inhibitors on clinical patient samples. All these efforts will contribute to understanding the mechanisms of HSP70 in cancer and translation of HSP70 inhibitors into clinical anti-cancer therapies.

Publications


  1. Rodina, A., Wang, T., Yan, P., Gomes, E. D., Dunphy, M. P. S., Pillarsetty, N., … Chiosis, G. (2016). The epichaperome is an integrated chaperome network that facilitates tumour survival. Nature, 538(7625), 397–401.

  2. Wu, W., Xu, C., Ling, X., Fan, C., Buckley, B. P., Chernov, M. V, … Wang, X. (2015). Targeting RING domains of Mdm2-MdmX E3 complex activates apoptotic arm of the p53 pathway in leukemia/lymphoma cells. Cell Death Dis, 6, e2035. (co-first author)

  3. Xu, C., Fan, C. D., & Wang, X. (2015). Regulation of Mdm2 protein stability and the p53 response by NEDD4-1 E3 ligase. Oncogene, 34(3), 281–289.

  4. Ling, X., Xu, C., Fan, C., Zhong, K., Li, F., & Wang, X. (2014). FL118 induces p53-dependent senescence in colorectal cancer cells by promoting degradation of MdmX. Cancer Research, 74(24), 7487–7497.

  5. Fan, C. D., Lum, M. A., Xu, C., Black, J. D., & Wang, X. (2013). Ubiquitin-dependent regulation of phospho-AKT Dynamics by the ubiquitin E3 LIGASE, NEDD4-1, in the insulin-like growth factor-1 response. Journal of Biological Chemistry, 288(3), 1674–1684.

  6. Xu, C., Yin, J. J., & Zhao, B. L. (2010). Structural characteristics of the hydrophobic patch of azurin and its interaction with p53: A site-directed spin labeling study. Science China Life Sciences, 53(10), 1181–1188.

  7. Xu, C., Zhao, Y., & Zhao, B. (2010). The interaction of azurin and C-terminal domain of p53 is mediated by nucleic acids. Archives of Biochemistry and Biophysics, 503(2), 223–229.