Mutant mice lacking the p53 C-terminal domain model telomere syndromes

Cell Rep. 2013 Jun 27;3(6):2046-58. doi: 10.1016/j.celrep.2013.05.028. Epub 2013 Jun 13.

Abstract

Mutations in p53, although frequent in human cancers, have not been implicated in telomere-related syndromes. Here, we show that homozygous mutant mice expressing p53Δ31, a p53 lacking the C-terminal domain, exhibit increased p53 activity and suffer from aplastic anemia and pulmonary fibrosis, hallmarks of syndromes caused by short telomeres. Indeed, p53Δ31/Δ31 mice had short telomeres and other phenotypic traits associated with the telomere disease dyskeratosis congenita and its severe variant the Hoyeraal-Hreidarsson syndrome. Heterozygous p53+/Δ31 mice were only mildly affected, but decreased levels of Mdm4, a negative regulator of p53, led to a dramatic aggravation of their symptoms. Importantly, several genes involved in telomere metabolism were downregulated in p53Δ31/Δ31 cells, including Dyskerin, Rtel1, and Tinf2, which are mutated in dyskeratosis congenita, and Terf1, which is implicated in aplastic anemia. Together, these data reveal that a truncating mutation can activate p53 and that p53 plays a major role in the regulation of telomere metabolism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Disease Models, Animal
  • Gene Expression
  • Humans
  • Male
  • Mice
  • Mice, Mutant Strains
  • Mutation
  • Protein Structure, Tertiary
  • Syndrome
  • Telomere / genetics*
  • Telomere / metabolism
  • Telomere / pathology
  • Telomere-Binding Proteins / genetics*
  • Telomere-Binding Proteins / metabolism
  • Tumor Suppressor Protein p53 / genetics*
  • Tumor Suppressor Protein p53 / metabolism

Substances

  • Telomere-Binding Proteins
  • Tumor Suppressor Protein p53