Polo-like kinase 1 facilitates loss of Pten tumor suppressor-induced prostate cancer formation

J Biol Chem. 2011 Oct 14;286(41):35795-35800. doi: 10.1074/jbc.C111.269050. Epub 2011 Sep 2.

Abstract

Loss of the tumor suppressor Pten (phosphatase and tensin homolog deleted on chromosome 10) is thought to mediate the majority of prostate cancers, but the molecular mechanism remains elusive. In this study, we demonstrate that Pten-depleted cells suffer from mitotic stress and that nuclear function of Pten, but not its phosphatase activity, is required to reverse this stress phenotype. Further, depletion of Pten results in elevated expression of Polo-like kinase 1 (Plk1), a critical regulator of the cell cycle. We show that overexpression of Plk1 correlates with genetic inactivation of Pten during prostate neoplasia formation. Significantly, we find that elevated Plk1 is critical for Pten-depleted cells to adapt to mitotic stress for survival and that reintroduction of wild-type Pten into Pten-null prostate cancer cells reduces the survival dependence on Plk1. We further show that Plk1 confers the tumorigenic competence of Pten-deleted prostate cancer cells in a mouse xenograft model. These findings identify a role of Plk1 in facilitating loss of Pten-induced prostate cancer formation, which suggests that Plk1 might be a promising target for prostate cancer patients with inactivating Pten mutations.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Line, Tumor
  • Cell Survival / genetics
  • Gene Deletion
  • Humans
  • Male
  • Mice
  • Mice, Nude
  • Mitosis*
  • Neoplasm Transplantation
  • PTEN Phosphohydrolase / genetics
  • PTEN Phosphohydrolase / metabolism*
  • Polo-Like Kinase 1
  • Prostatic Neoplasms / enzymology*
  • Prostatic Neoplasms / therapy
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*
  • Proto-Oncogene Proteins / genetics
  • Proto-Oncogene Proteins / metabolism*
  • Stress, Physiological / genetics
  • Transplantation, Heterologous

Substances

  • Cell Cycle Proteins
  • Proto-Oncogene Proteins
  • Protein Serine-Threonine Kinases
  • PTEN Phosphohydrolase
  • PTEN protein, human
  • Pten protein, mouse