The tumor suppressor RECK interferes with HER-2/Neu dimerization and attenuates its oncogenic signaling

FEBS Lett. 2011 Feb 18;585(4):591-5. doi: 10.1016/j.febslet.2011.01.021. Epub 2011 Jan 19.

Abstract

Our previous study demonstrates that HER-2/Neu oncogene inhibits a matrix metalloproteinase inhibitor and tumor metastasis suppressor RECK to promote metastasis. Conversely, the effect of RECK on the oncogenic function of HER-2/Neu is unknown. Ectopic expression of RECK in 293T cells and HER-2/Neu-overexpressing breast cancer cells shows that RECK and HER-2/Neu are co-localized and these two proteins can be co-immunoprecipitated. RECK inhibits HER-2/Neu receptor dimerization and autophosphorylation, which causes reduction of ERK and AKT kinase activity and down-regulation of HER-2/Neu target genes. RECK expression is reduced in 58.8% of breast cancer tissues and is associated with lymph node invasion supporting its anti-metastatic role. Collectively, we provide the first evidence that RECK can negatively regulate oncogenic activity of HER-2/Neu by inhibiting receptor dimerization.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Breast Neoplasms / metabolism*
  • Breast Neoplasms / pathology
  • Cell Line
  • Cell Line, Tumor
  • Cell Proliferation
  • Down-Regulation*
  • Female
  • GPI-Linked Proteins / genetics
  • GPI-Linked Proteins / metabolism*
  • Gene Expression Regulation, Neoplastic
  • Humans
  • Immunoprecipitation
  • Lymphatic Metastasis
  • Medical Records
  • Neoplasm Staging
  • Phosphorylation
  • Protein Multimerization*
  • Protein Transport
  • RNA, Messenger
  • Receptor, ErbB-2 / genetics
  • Receptor, ErbB-2 / metabolism*
  • Recombinant Proteins / metabolism
  • Signal Transduction*

Substances

  • GPI-Linked Proteins
  • RECK protein, human
  • RNA, Messenger
  • Recombinant Proteins
  • ERBB2 protein, human
  • Receptor, ErbB-2