EGFR activation and signaling in cancer cells are enhanced by the membrane-bound metalloprotease MT4-MMP

Cancer Res. 2014 Dec 1;74(23):6758-70. doi: 10.1158/0008-5472.CAN-13-2994. Epub 2014 Oct 15.

Abstract

MT4-MMP (MMP-17) is a glycosylphosphatidyl inositol-anchored matrix metalloprotease expressed on the surface of cancer cells that promotes tumor growth and metastasis. In this report, we identify MT4-MMP as an important driver of cancer cell proliferation through CDK4 activation and retinoblastoma protein inactivation. We also determine a functional link between MT4-MMP and the growth factor receptor EGFR. Mechanistic experiments revealed direct association of MT4-MMP and its positive effects on EGFR phosphorylation in response to TGFα and EGF in cancer cells. Notably, the effects of MT4-MMP on proliferation and EGFR activation did not rely on metalloprotease activity. Clinically, MT4-MMP and EGFR expressions were correlated in human triple-negative breast cancer specimens. Altogether, our results identify MT4-MMP as a positive modifier of EGFR outside-in signaling that acts to cooperatively drive cancer cell proliferation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Breast Neoplasms / metabolism*
  • COS Cells
  • Cell Line, Tumor
  • Cell Membrane / metabolism*
  • Cell Proliferation / physiology
  • Chlorocebus aethiops
  • Cyclin-Dependent Kinase 4 / metabolism
  • Epidermal Growth Factor / metabolism
  • ErbB Receptors / metabolism*
  • Female
  • HeLa Cells
  • Humans
  • Matrix Metalloproteinases, Membrane-Associated / metabolism*
  • Mice
  • Retinoblastoma Protein / metabolism
  • Signal Transduction / physiology*
  • Transforming Growth Factor alpha / metabolism
  • Triple Negative Breast Neoplasms / metabolism

Substances

  • Retinoblastoma Protein
  • Transforming Growth Factor alpha
  • Epidermal Growth Factor
  • EGFR protein, human
  • ErbB Receptors
  • CDK4 protein, human
  • Cyclin-Dependent Kinase 4
  • MMP17 protein, human
  • Matrix Metalloproteinases, Membrane-Associated