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Pharmacological inhibition of BMK1 suppresses tumor growth through promyelocytic leukemia protein.

BMK1 is activated by mitogens and oncogenic signals and, thus, is strongly implicated in tumorigenesis. We found that BMK1 interacted with promyelocytic leukemia protein (PML), and inhibited its tumor-suppressor function through phosphorylation. Furthermore, activated BMK1 notably inhibited PML-dependent activation of p21. To further investigate the BMK-mediated inhibition of the tumor suppressor activity of PML in tumor cells, we developed a small-molecule inhibitor of the kinase activity of BMK1, XMD8-92. Inhibition of BMK1 by XMD8-92 blocked tumor cell proliferation in vitro and significantly inhibited tumor growth in vivo by 95%, demonstrating the efficacy and tolerability of BMK1-targeted cancer treatment in animals.

Pubmed ID: 20832753


  • Yang Q
  • Deng X
  • Lu B
  • Cameron M
  • Fearns C
  • Patricelli MP
  • Yates JR
  • Gray NS
  • Lee JD


Cancer cell

Publication Data

September 14, 2010

Associated Grants

  • Agency: NCI NIH HHS, Id: CA079871
  • Agency: NCI NIH HHS, Id: CA114059
  • Agency: NCI NIH HHS, Id: R01 CA079871-08
  • Agency: NCI NIH HHS, Id: R01 CA079871-09
  • Agency: NCI NIH HHS, Id: R01 CA079871-10
  • Agency: NCI NIH HHS, Id: R01 CA114059-03
  • Agency: NCI NIH HHS, Id: R01 CA114059-04
  • Agency: NCI NIH HHS, Id: R01 CA114059-05

Mesh Terms

  • Animals
  • Cell Growth Processes
  • Cell Nucleus
  • Cytosol
  • Genes, Tumor Suppressor
  • HeLa Cells
  • Humans
  • Mitogen-Activated Protein Kinase 7
  • Neoplasms
  • Nuclear Proteins
  • Phosphorylation
  • Protein Kinase Inhibitors
  • Signal Transduction
  • Transcription Factors
  • Tumor Suppressor Proteins