Regulation of p53 protein function through alterations in protein-folding pathways

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The tumour suppressor protein p53 is a stress-activated transcription factor whose activity is required for regulating the cellular response to stress and damage. The biochemical activity of p53 as a transcription factor can be regulated by partner proteins affecting stability, nuclear transport, signalling pathways modulating phosphorylation and interactions with components of the transcriptional machinery. The key structural determinants of p53 protein that drive sequence-specific DNA binding include the core specific DNA-binding domain and the tetramerization domain. Flanking these domains are more evolutionarily divergent carboxy- and amino-terminal regulatory motifs that further modulate tetramerization and sequence-specific transactivation. This review will mainly focus on the mechanisms whereby the tetramerization domain modulates sequence-specific DNA binding and how missense point mutations in p53 protein and the activity of molecular chaperones may lead to unfolding of mutant p53 tetramers in human tumours.
Original languageEnglish
Pages (from-to)88-95
Number of pages8
JournalCellular and Molecular Life Sciences
Issue number1
Publication statusPublished - Jan 1999

Keywords / Materials (for Non-textual outputs)

  • Antigens, Viral, Tumor
  • DNA-Binding Proteins
  • Gene Expression Regulation
  • Molecular Chaperones
  • Phosphorylation
  • Point Mutation
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Tumor Suppressor Protein p53


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