Contact Information
Address (Office) E12-3028 Vivien WANG
(Lab) N22-3038
Phone (Office) 8822 4933
(Lab) 8822 2950
Fax 8822 2314
Email VivienWang@umac.mo
Education
Ph.D. Department of Chemistry and Biochemistry, University of California San Diego, USA (2011)
M.Sc. Department of Chemistry and Biochemistry, University of California San Diego, USA (2008)
B.Sc. Department of Chemistry and Biochemistry, University of California San Diego, USA (2005)
Positions
2016.8-present Assistant Professor, Faculty of Health Sciences, University of Macau
2015.9-2016.8 Visiting Assistant Professor, Faculty of Health Sciences, University of Macau
2015.3-2015.8 Visiting Scientist, Department of Chemistry and Biochemistry, University of California San Diego, USA
2012.9-2015.3 Postdoc Research Fellow, Department of Biological Sciences, Columbia University, New York, USA
2011.7-2012.9 Postdoc Research Fellow, Department of Chemistry and Biochemistry, University of California San Diego, USA
Research Interests

In this laboratory we use our knowledge and experience in the area of biochemistry, structural biology, cellular and molecular biology to study the functions and mechanisms of important molecules focusing on their biological functions. The major focus of the current research involves understanding the signal transduction mediated by the nuclear factor kappaB (NF-kB) and IkB proteins. The mammalian Rel/NF-kB family of transcription factors plays a critical role in diverse physiological processes including the immune response, inflammation, cell proliferation and survival. A wide variety of signals activate NF-kB driven gene expression through different NF-kB signaling pathways in a stimulus- and cell type-dependent manner. Due to the diverse regulatory mechanisms acting on NF-kB, the signal dependent activation of NF-kB remains a challenging area of research. Using both biochemical and structural approaches, we will determine how post-translational modifications, e.g. phosphorylation, affect NF-kB:IkB:DNA complex formation, binding specificity, and target gene expression.

Representative Publications
  • Mulero, M.C., Shahabi, S., Ko, M.S., Schiffer, J.M., Huang, D-B., Wang, V.Y., Amaro, R.E., Huxford, T., Ghosh, G. Protein Cofactors Are Essential for High-Affinity DNA Binding by the Nuclear Factor κB RelA Subunit. Biochemistry. 2018, 57(20):2943-2957. DOI:10.1021/acs.biochem.8b00158.
  • Mulero, M.C., Huang, D-B., Nguyen, H.T., Wang, V.Y., Li, Y., Biswas, T., Ghosh, G. DNA-binding affinity and transcriptional activity of the RelA homodimer of nuclear factor κB are not correlated. J Mol Biol. 2017, 292(46):18821-18830. DOI:10.1074/jbc.M117.813980.
  • Wang, V.Y., Li Y., Kim, D., Zhong, X.Y., Ghassemian, M., and Ghosh, G. Bcl3 Phosphorylation by Akt, Erk2 and IKK1 is Required for Its Activation. Mol Cell2017, 67(1), 1-14. DOI: https://doi.org/10.1016/j.molcel.2017.06.011.
  • Fusco, A.J., Mazumder, A., Wang, V.Y., Tao, Z., Ware, C., and Ghosh, G. The NF-κB subunit RelB controls p100 processing by competing with the kinases NIK and IKK1 for binding to p100. Sci Signal. 2016, 9(447):ra96. DOI: 10.1126/scisignal.aad9413.
  • Sansó, M., Levin, RS., Lipp JJ, Wang, V.Y., Greifenberg, AK., Quezada, EM., Ali, A., Ghosh, A., Larochelle, S., Rana, TM., Geyer, M., Tong, L., Shokat, KM., Fisher, RP. P-TEFb regulation of transcription termination factor Xrn2 revealed by a chemical genetic screen for Cdk9 substrates. Genes Dev. 2016, 30(1), 117-131.
  • Wang, V.Y., Jiao, X., Kiledjian, M., and Tong, L. Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes. Nucleic Acids Res. 2015, 43(13), 6596-6606.
  • Wang, V.Y., Huang, W., Asagiri, M., Spann, N., Hoffmann, A., Glass, C., and Ghosh, G. The transcriptional specificity of NF-kB Dimers is coded within the kB DNA Response elements. Cell Rep. 2012, 2(4), 824-839.
  • Ghosh, G., Wang, V.Y., Huang, D-B., and Fusco, A.J. NF-kB Regulation: Lessons from Structures. Immunological Rev. 2012, 246, 36-58.
  • Fusco, A.J., Huang, D-B., Miller, D., Wang, V.Y., Vu, D., and Ghosh, G. NF-kappaB p52:RelB heterodimer recognizes two classes of kappaB sites with two distinct modes. EMBO Rep. 2009, 10, 152-159.
  • Moorthy, A.K., Huang, D-B., Wang, V.Y., Vu, D., and Ghosh, G. X-ray structure of a NFkappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites. J Mol Biol. 2007, 373, 723-734.
  • Moorthy, A.K., Savinova, O.V., Ho, J.Q., Wang, V.Y., Vu, D., and Ghosh, G. The 20S proteasome processes NF-kappaB1 p105 into p50 in a translation-independent manner. EMBO J. 2006, 25, 1945-1956.