Shengyu Yang, PhD

Where You Are:
Shengyu Yang, PhD

Assistant Member

Office  (813) 745-8371

Education And Training
  • Postdoctoral Fellow, Cornell University Weill Medical College, 2010 - Physiology and Biophysics
  • PhD, Chinese Academy of Sciences, 2001 - Biochemistry and Molecular Biology


Our long term goal is to reveal the mechanisms by which the deregulated actin cytoskeleton promotes cancer metastasis and to develop anti-metastasis agents targeting the deregulated actin cytoskeleton in metastatic cancer cells.   One critical characteristic of metastatic cancer cells is enhanced migration and invasion, which are responsible for the infiltration of metastatic cells into lymphatic and blood vessels, as well as the extravasation of cancer cells into secondary organs.  The driving forces of cell migration and invasion are conferred by the actin cytoskeleton and focal adhesions that anchor actin filaments to the extracellular matrix. The researches in our lab currently focus on two interrelated projects. The first project is about fascin, an actin bundling protein. Fascin expression is very low in normal epithelia, but highly elevated in all forms of carcinoma. More importantly, high fascin levels independently predict poor clinical outcome in cancer patients. We are currently exploring the mechanism that regulates fascin expression and activity in metastatic cells. The second project is about store-operated calcium channels. We discovered that store-operared calcium channels are required for actin cytoskeleton remodeling during cancer metastasis and we are currently looking into signaling pathways downstream of calcium signaling.

The Yang lab long-term goal is to reveal the mechanisms by which the deregulated actin cytoskeleton promotes cancer metastasis and to develop anti-metastasis agents targeting the deregulated actin cytoskeleton in metastatic cancer cells.  The researches in our lab currently focus on two interrelated projects. The first project is about exploring the mechanism by which fascin expression and activity in metastatic cells are regulated. The second project is about store-operated calcium channels. We discovered that store-operated calcium channels are required for actin cytoskeleton remodeling during cancer metastasis and we are currently looking into signaling pathways downstream of calcium signaling.

  • Sun J, He H, Pillai S, Xiong Y, Challa S, Xu L, Chellappan S, Yang S. GATA3 transcription factor abrogates Smad4 transcription factor-mediated fascin overexpression, invadopodium formation, and breast cancer cell invasion. J Biol Chem. 2013 Dec;288(52):36971-36982. Pubmedid: 24235142. Pmcid: PMC3873555.
  • Sun J, He H, Xiong Y, Lu S, Shen J, Cheng A, Chang WC, Hou MF, Lancaster JM, Kim M, Yang S. Fascin protein is critical for transforming growth factor β protein-induced invasion and filopodia formation in spindle-shaped tumor cells. J Biol Chem. 2011 Nov;286(45):38865-38875. Pubmedid: 21914811. Pmcid: PMC3234711.
  • Chen L, Yang S, Jakoncic J, Zhang JJ, Huang XY. Migrastatin analogues target fascin to block tumour metastasis. Nature. 2010 Apr;464(7291):1062-1066. Pubmedid: 20393565. Pmcid: PMC2857318.
  • Yang S, Zhang JJ, Huang XY. Orai1 and STIM1 are critical for breast tumor cell migration and metastasis. Cancer Cell. 2009 Feb;15(2):124-134. Pubmedid: 19185847.
  • McGarrigle D, Shan D, Yang S, Huang XY. Role of tyrosine kinase Csk in G protein-coupled receptor- and receptor tyrosine kinase-induced fibroblast cell migration. J Biol Chem. 2006 Apr;281(15):10583-10588. Pubmedid: 16501257.
  • Yang S, Huang XY. Ca2+ influx through L-type Ca2+ channels controls the trailing tail contraction in growth factor-induced fibroblast cell migration. J Biol Chem. 2005 Jul;280(29):27130-27137. Pubmedid: 15911622.
  • Yang S, Zhang L, Huang Y. Membrane association and conformational change of palmitoylated G(o)alpha. FEBS Lett. 2001 Jun;498(1):76-81. Pubmedid: 11389902.
  • Zhang L, Yang S, Huang Y. Evidence for disaggregation of oligomeric G(o)alpha induced by guanosine-5;-3-O-(thio)triphosphate activation. Biochemistry (Mosc). 2003 Jan;68(1):121-128. Pubmedid: 12693986.
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