PHGDH amplification and altered glucose metabolism in human melanoma

Authors

  • Edouard Mullarky,

    1.  Division of Signal Transduction, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA
    2.  Department of Systems Biology, Harvard Medical School, Boston, MA 02215, USA
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  • Katherine R. Mattaini,

    1.  Kock Institute for Integrative Cancer Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
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  • Matthew G. Vander Heiden,

    1.  Kock Institute for Integrative Cancer Research, Department of Biology, Massachusetts Institute of Technology, Cambridge, MA 02139, USA
    2.  Department of Medical Oncology, Dana Farber Cancer Institute, Harvard Medical School, Boston, MA 02215, USA
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  • Lewis C. Cantley,

    1.  Division of Signal Transduction, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA
    2.  Department of Systems Biology, Harvard Medical School, Boston, MA 02215, USA
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  • Jason W. Locasale

    1.  Division of Signal Transduction, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA
    2.  Department of Systems Biology, Harvard Medical School, Boston, MA 02215, USA
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J. W. Locasale, e-mail: jlocasal@bidmc.harvard.edu

Summary

The metabolic requirements of cancer cells differ from that of their normal counterparts. To support their proliferation, cancer cells switch to a fermentative metabolism that is thought to support biomass production. Instances where metabolic enzymes promote tumorigenesis remain rare. However, an enzyme involved in the de novo synthesis of serine, 3-phosphoglycerate dehydrogenase (PHGDH), was recently identified as a putative oncogene. The potential mechanisms by which PHGDH promotes cancer are discussed.

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