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Department of Chemistry and Chemical Biology

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Faculty Detail

Cerione, Richard A

Goldwin Smith Professor

phone: 607/253-3888
room: Vet Medical Center, Room C3

Department Appointments

  • Cerione, Richard A
  • Molecular Medicine JM
  • Molecular Medicine DEPT JM
  • Molecular Medicine SUBD
  • Molecular Medicine DEPT

Graduate Fields

  • Biochemistry, Molecular and Cell Biology
  • Biophysics
  • Chemistry and Chemical Biology
  • Comparative Biomedical Sciences
  • Neurobiology and Behavior
  • Pharmacology
  • Tri-Institutional Training Program in Chemical Biology (TPCB)

Other Affiliations

  • Weill Institute for Cell and Molecular Biology Advisory Committee
  • Cornell High Energy Synchrotron Source (CHESS)
  • Macromolecular Diffraction Facility at Cornell High Energy Synchrotron Source (MacCHESS)


Multi-component signal transduction pathways that influence cell growth and differentiation


The Cerione group is studying signaling pathways that are important in various biological outcomes, with particular emphasis on cancer progression and neurogenesis.  They are using a combination of biochemical, structural, genetic, and small molecule chemistry to probe these pathways.


The research efforts of my laboratory have focused on understanding how cellular signaling pathways influence cell growth and differentiation, as well as how aberrant signaling activities lead to disease states such as cancer and other disorders.  The laboratory is multi-disciplinary using various cell systems and mouse models to identify novel signaling events that influence fundamentally important biological processes, and chemistry and structural approaches to define the molecular basis for these events.  Three major areas of interest are currently being pursued.

The first involves the development and application of structural methods to gain a more complete picture of how G proteins become activated and transmit signals within the context of the cell membrane.  The second involves the use of small molecule chemistry to identify novel pathways necessary to satisfy the bioenergetics and metabolic requirement of cancer cells to proliferate at high rates and become invasive, with the ultimate goal of defining new strategies for therapeutic intervention.  The third focuses on the recent identification of a new class of membrane vesicles that are shed by cancer cells and stem cells, with the goal being to understand how these vesicles play critical roles in the development of the malignant state and in stem cell biology.

Selected Publications

Katt, W.P., and Cerione, R.A. (2013) Glutaminase regulation in cancer cells:  a druggable chain of events.  Drug Discov. Today S1359-6446, 00334-00336.

Lukey, M.J., Wilson, K.F., and Cerione, R.A. (2013) Therapeutic strategies impacting cancer cell glutamine metabolism.  Future Med. Chem. 5, 1685-1700.  PMC Journal – In Process.

Zhang, J., Antonyak, M.A., Singh, G., and Cerione, R.A. (2013) A mechanism for the upregulation of EGF receptor levels in glioblastomas.  Cell Rep. 3, 2008-2020. PMCID: PMC3742030

Wilson, K.F., Erickson, J.W., Antonyak, M.A., and Cerione, R.A. (2013) Rho GTPases and their roles in cancer metabolism.  Trends Mol. Med.  19, 74-82.  PMCID: PMC3607349

Katt, W.P., Ramachandran, S., Erickson, J.W., and Cerione, R.A. (2012) Dibenzophenanthridines as inhibitors of glutaminase C and cancer cell proliferation.  Mol. Cancer Ther. 11, 1269-1278.  PMCID: PMC3620022

Johnson, J., Erickson, J.W., and Cerione, R.A. (2012) C-terminal di-arginine motif of Cdc42 protein is essential for binding to phosphatidylinositol 4,5 bisphosphate-containing membranes and inducing cellular transformation.  J. Biol. Chem. 287, 5764-5774.  PMCID: PMC3325590

Li, B., Antonyak, M.A., Zhang, J., and Cerione, R.A. (2012) RhoA triggers a specific signaling pathway that generates transforming microvesicles in cancer cells. Oncogene 31, 4740-4749.  PMCID: PMC3607381

Antonyak, M.A., Li, B., Boroughs, L.K., Johnson, J.L., Druso, J.E., Bryant, K.L., Holowka, D.A., and Cerione, R.A. (2011) Cancer cell-derived microvesicles induce transformation by transferring tissue transglutaminase and fibronectin to recipient cells.  Proc. Natl. Acad. Sci. USA 108, 4852-4857.  PMCID: PMC3064359  Highlight Article

Erickson, J.W., and Cerione, R.A. (2010) Glutaminase:  A hot spot for regulation of cancer cell metabolism?  Oncotarget 1, 734-740.  PMCID: PMC3018840

Wang, J.B., Erickson, J.W., Fuji, R., Ramachandran, S., Gao, P., Dinavahi, R., Wilson, K.F., Ambrosio, A.L.B., Dias, S.M.G., Dang, C.V., and Cerione, R.A. (2010) Targeting mitochondrial glutaminase activity inhibits oncogenic transformation.  Cancer Cell 18, 207-219.  PMCID: PMC3078749  Cover Article

Dias, S.M.G., Wilson, K.F., Rojas, K.S., Ambrosio, A.L.B., and Cerione, R.A. (2009) The molecular basis for the regulation of the cap-binding complex by the importins.  Nat. Struct. Mol. Biol. 16, 930-937.  PMCID: PMC2782468

Endo, M., Antonyak, M.A., and Cerione, R.A. (2009) Cdc42-mTOR signaling pathway controls Hes5 and Pax6 expression in retinoic acid-dependent neural differentiation.  J. Biol. Chem. 284, 5107-5118.  PMID: 19097998  Cover Article