Allosteric activation of latent p53 tetramers

T R Hupp, D P Lane

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

The DNA-binding activity of p53 is essential to its function as a tumour suppressor. Point mutations that abolish this activity have been found to occur frequently in the p53 genes of human cancer cells. Wild-type p53 protein assembles into oligomers with latent DNA-binding activity that can be activated in vitro by phosphorylation of a carboxy-terminal regulatory region, catalyzed by protein kinase C or casein kinase II. We have investigated the mechanism underlying this post-translational regulation of p53. Specifically, we have asked the following questions. First, whether the carboxy-terminal regulatory site contributes to p53's ability to form tetramers. Second, whether the latent DNA-binding activity of p53 can be activated in vivo. And third, whether the activation of p53 is reversible.
Original languageEnglish
Pages (from-to)865-75
Number of pages11
JournalCurrent biology : CB
Issue number10
Publication statusPublished - 1 Oct 1994

Keywords / Materials (for Non-textual outputs)

  • Allosteric Regulation
  • Amino Acid Sequence
  • Animals
  • Antibodies, Monoclonal
  • Cell Line
  • DNA
  • Humans
  • Molecular Sequence Data
  • Phosphorylation
  • Tumor Suppressor Protein p53


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