The proline-rich domain of p53 is required for cooperation with anti-neoplastic agents to promote apoptosis of tumor cells

Oncogene. 2002 Jan 3;21(1):9-21. doi: 10.1038/sj.onc.1205015.

Abstract

In some cell types either DNA damage or p53 expression leads to minimal cell death, while combining the two leads to a strong apoptotic response. To further understand features of p53 that contribute to this increased cell death we used clones of H1299 cells that express wild-type or several mutant forms of p53 under a tetracycline-regulated promoter. In these cells the induction of wild-type p53 leads to significant apoptosis only when combined with exposure to a number of chemotherapeutic agents. A common target of p53, p21, is itself not sufficient to cause apoptosis in the presence of these chemotherapeutic compounds. Many agents also effectively increase cell death when a transcriptionally-defective p53, p53([gln22ser23]), is induced, although a dramatic exception is treatment with 5-FU, which strongly cooperates with wild-type but not p53([gln22ser23]). Our results with 5-FU thus show that genetically separable functions of p53 are involved in its ability to respond to DNA-damaging agents to induce apoptosis. Notably as well, deleting the C-terminal 30 amino acids of p53 does not affect this cooperative effect with DNA-damaging agents. By contrast, a p53 mutant lacking the PXXP-domain between residues 60-90, while at least partially transcriptionally-competent, cannot be rendered apoptotic by any compounds that we tested. Thus the PXXP domain provides an essential component of the ability of p53 to respond to DNA-damaging agents to cause cell death.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antineoplastic Agents / pharmacology*
  • Apoptosis / drug effects
  • Apoptosis / physiology*
  • Camptothecin / pharmacology
  • Carcinoma, Non-Small-Cell Lung / pathology
  • Cell Cycle / drug effects
  • Clone Cells / drug effects
  • Clone Cells / metabolism
  • Colchicine / pharmacology
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins / physiology
  • DNA Damage
  • DNA, Neoplasm / drug effects
  • DNA, Neoplasm / genetics
  • Daunorubicin / pharmacology
  • Etoposide / pharmacology
  • Fluorouracil / pharmacology
  • Gene Expression Regulation, Neoplastic / drug effects
  • Gene Expression Regulation, Neoplastic / physiology
  • Genes, p53
  • Humans
  • Lung Neoplasms / pathology
  • Models, Biological
  • Proline / chemistry*
  • Promoter Regions, Genetic
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / physiology
  • Structure-Activity Relationship
  • Tetracycline / pharmacology
  • Transcription, Genetic
  • Tumor Cells, Cultured / drug effects
  • Tumor Cells, Cultured / metabolism
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / physiology*

Substances

  • Antineoplastic Agents
  • CDKN1A protein, human
  • Cyclin-Dependent Kinase Inhibitor p21
  • Cyclins
  • DNA, Neoplasm
  • Recombinant Fusion Proteins
  • Tumor Suppressor Protein p53
  • Etoposide
  • Proline
  • Tetracycline
  • Colchicine
  • Fluorouracil
  • Camptothecin
  • Daunorubicin