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Kong-Mei

Mei Kong, Ph.D.

  • Assistant Professor, Department of Cancer Biology

Mei Kong, Ph.D.

Research Focus :
  • Cancer Biology
  • Cell Signaling
  • Cancer Metabolism
Languages Spoken
  • Mandarin
  • 2010 - present, Faculty Member, City of Hope's Irell & Manell Graduate School of Biological Sciences, Duarte, CA
  • 2016 - Present, Associate professor, Department of Cancer Biology, Beckman Research Institute, City of Hope
  • 2010 - 2016, Assistant professor, Department of Cancer Biology, Beckman Research Institute, City of Hope
  • 2009 - 2010, Research Associate, Department of Cancer Biology, University of Pennsylvania, Pennsylvania, PA


2003, McGill University, Montreal, Canada, Experimental Medicine, Ph.D.

Fellowship

  • 2003 - 2009, Abramson Family Cancer Research Institute, University of Pennsylvania, Pennsylvania, PA, Cancer Biology, Postdoctoral Fellow
  • 2003 - 2009, Abramson Family Cancer Research Institute, University of Pennsylvania, Pennsylvania, PA, Cancer Biology, Postdoctoral Fellow

Signal transduction and Cancer Metabolism
Our laboratory is interested to delineate strategies used by tumor cells to survive temporary periods of nutrient deprivation and then to develop novel therapies targeting nutrient-sensing pathways of neoplastic cells.  Tumor cells often display fundamental changes in metabolism and increase their uptake of nutrients to meet the increased bioenergetic demands of proliferation.  Glucose and glutamine are two main nutrients whose uptake is directly controlled by signal transduction and are essential for tumor cell survival and proliferation.  Altered glucose metabolism in cancer cells is termed the Warburg effect, which describes the propensity of most cancer cells to take up glucose avidly and convert it primarily to lactate, despite available oxygen.   In addition to glucose, glutamine is another essential nutrient whose uptake is directly controlled by oncogenes, and it is critical for cancer cell survival and proliferation.  During tumor growth, increased uptake of nutrients and rapid accumulation of cells can outstrip the supply of essential nutrients, including glucose and glutamine.  How tumor cells survive these temporary periods of nutrient deprivation is unclear, but is necessary for tumorigenesis to persist.  The major goal of our laboratory is to delineate the strategies, including signaling pathways, epigenetic modifications and metabolic alterations,  used by tumor cells to survive periods of nutrient deprivation and then to develop novel therapies targeting nutrient-sensing pathways of neoplastic cells.  

Protein Phosphatase 2A Complexes in Cancer
Reversible protein phosphorylation is the major regulatory mechanism used by cells to respond to environmental and nutritional stresses.  Aberrant regulation of this activity leads to dysregulated cellular behavior and disease phenotypes, including many forms of cancer. Although we know much about how protein kinases function in specific signaling governed by phosphorylation, whether protein phosphatases are also regulated and actively function in the process to counteract kinase function has not been established. Protein phosphatase 2A (PP2A) is a major serine/threonine phosphatase that regulates many signaling pathways. Unlike kinases, serine/threonine phosphatases are promiscuously active and their specificity is governed largely by associated proteins. Thus, the specificity of PP2A is conferred by assembly of a trimeric complex including a catalytic C subunit, a scaffolding A subunit, and one of the sixteen regulatory B subunits. In addition to interacting with conventional A and B subunits, the C subunit reportedly forms two other distinct complexes with proteins designated 4 (Tap42 in yeast) and Tiprl (Tip41 in yeast).  Our laboratory also interested in characterizing molecular mechanisms underlying the response of PP2A complexes to stress signals and understanding the role of PP2A regulatory subunit in cancer. 

  • Rosales KR, Reid MA, Yang Y, Tran TQ, Wang WI, Lowman X,  Pan M and Kong M. TIPRL Inhibits Protein Phosphatase 4 Activity and Promotes H2AX Phosphorylation in the DNA Damage Response. PLoS One. 2015 Dec 30
  • Fong MY, Zhou W, Liu L, Alontaga AY, Chandra M, Ashby J, Chow A, O'Connor ST, Li S, Chin AR, Somlo G, Palomares M, Li Z, Tremblay JR, Tsuyada A, Sun G, Reid MA, Wu X, Swiderski P, Ren X, Shi Y, Kong M, Zhong W, Chen Y, Wang SE. Breast-cancer-secreted miR-122 reprograms glucose metabolism in premetastatic niche to promote metastasis. Nature Cell Biology, 2015 Jan 26. doi: 10.1038/ncb3094.
  • Hernandez-Davies JE, Tran TQ, Reid MA, Rosales KR, Lowman XH, Pan M, Moriceau G, Yang Y, Wu J, Lo RS, Kong M. Vemurafenib resistance reprograms melanoma cells towards glutamine dependence.  J Transl Med. 2015 Jul 3;13(1):210. doi: 10.1186/s12967-015-0581-2. PMID: 26139106
  • Reid M.A., Wang W.I., Rosales K.R., Welliver M.X., Pan M., and Kong M. The B55 subunit of PP2A drives a p53-dependent metabolic adaptation to glutamine deprivation. Molecular Cell, 2013 50(2):200-211.
  • Jiang L., Stanevich V., Satyshur K.A., Kong M., Watkins G.R., Wadzinski B.E., Sengupta R., and Xing Y. (2013). Structural basis of protein phosphatase 2A stable latency. Nat Commun, Epub, 2013 Apr 16;4:1699. doi: 10.1038/ncomms2663
  • Lum JJ, Bauer DE, Kong M, Harris MH, Li C, Lindsten T, Thompson CB. Growth factor regulation of autophagy and cell survival in the absence of apoptosis. Cell 120, 237-48 (2005)
  • Lin T.C., Chen Y.R., Kensicki E., Li A.Y., Kong M., Li Y., Mohney R.P., Shen H.M., Stiles B., Mizushima N., Lin L.I., & Ann D.K. Autophagy: Resetting glutamine-dependent metabolism and oxygen consumption. Autophagy, 2012 8(10): 1477-1493
  • Kong M, Ditsworth D, Lindsten T, and Thompson CB.  4 is an essential regulator of PP2A phosphatase activity. Molecular Cell, 2009, 36:51-60
  • Gruber J, Yong J, Zatechka DS, Sabin L, Zhang Z, Lum JJ, Kong M, Zong WX, Lau CK, Cherry S, Ihle J,  Dreyfuss G, and Thompson CB. Ars2 links the nuclear cap binding complex to RNA interference and cell proliferation. Cell  138:328-39, (2009)
  • Kong M, Bui TV,  Ditsworth D, Gruber JJ,  Goncharov D,  Krymskaya VP,  Lindsten T,  and Thompson CB.  The PP2A-associated protein 4 plays a critical role in the regulation of cell spreading and migration. J. Biol. Chem. 282, 29712-20, (2007)
  • Kong M, Fox CJ, Mu J, Solt L, Xu A, Cinalli RM, Birnbaum MJ, Lindsten T, Thompson CB. The PP2A-associated protein 4 is an essential inhibitor of apoptosis. Science 306, 695-8 (2004)
  • Kong M, Mounier C, Dumas V, Posner BI. Gab2 tyrosine phosphorylation by a pleckstrin homology domain-independent mechanism: role in epidermal growth factor-induced mitogenesis. Mol. Endocrinol. 17, 935-44 (2003)
  • Kong M, Mounier C, Balbis A, Baquiran G, Posner BI. Epidermal growth factor-induced DNA synthesis. Key role for Src phosphorylation of the docking protein Gab2. J. Biol. Chem. 278, 5837-44 (2003).
  • Kong M, Mounier C, Wu J, Posner BI. Epidermal growth factor-induced phosphatidylinositol 3-kinase activation and DNA synthesis: Identification of Grb2-associated binder 2 as the major mediator in rat hepatocytes.  J. Biol. Chem. 275, 36035-42 (2000)
  • Lavoie L, Band CJ, Kong M, Bergeron JJ, Posner BI.  Regulation of glycogen synthase in rat hepatocytes: Evidence for multiple signaling pathways. J. Biol. Chem. 274, 28279-85 (1999)
  • 2010 - present, Active member of the American Association for Cancer Research (AACR) and AACR-Women in Cancer Research (WICR)
  • 2016, Research Scholar, American Cancer Society
  • 2015, Stand Up to Cancer Phillip A. Sharp Innovation in Collaboration Award
  • 2013, V Scholar, V Foundation for Cancer Research
  • 2011, Pew Scholar in Biomedical Research, Pew Trust
  • 2011, Innovative Research Grant Award, Stand Up to Cancer/ AACR
  • 2011, Sidney Kimmel Scholar in Cancer Research, Sidney Kimmel Foundation
  • 2010, Research Career Development Award, STOP CANCER
  • 2007, Career Development Award (Special Fellow), the Leukemia and Lymphoma Society
  • 2006, AACR Postdoctoral Fellowship in Cancer Research
  • 2004, Postdoctoral Fellowship, Lymphoma Research Foundation
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