Amino-terminal residues of Δnp63, mutated in ectodermal dysplasia, are required for its transcriptional activity

Anna Maria Lena, Sara Duca, Flavia Novelli, Sonia Melino, Margherita Annicchiarico-Petruzzelli, Gerry Melino, Eleonora Candi

Research output: Contribution to journalArticle


p63, a member of the p53 family, is a crucial transcription factor for epithelial development and skin homeostasis. Heterozygous mutations in TP63 gene have been associated with human ectodermal dysplasia disorders. Most of these TP63 mutations are missense mutations causing amino acidic substitutions at p63 DNA binding or SAM domains that reduce or abolish the transcriptional activity of mutants p63. A significant number of mutants, however, resides in part of the p63 protein that apparently do not affect DNA binding and/or transcriptional activity, such as the N-terminal domain. Here, we characterize five p63 mutations at the 5′ end of TP63 gene aiming to understand the pathogenesis of the diseases and to uncover the role of ΔNp63α N-terminus residues in determining its transactivation potential.

Original languageEnglish
Pages (from-to)434-440
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number2
Publication statusPublished - Nov 13 2015



  • AEC
  • Ankyloblepharon-Ectodermal defects-cleft lip/palate syndrome
  • Ectodermal dysplasia
  • Ectrodactyly-Ectodermal dysplasia and cleft lip/palate syndrome
  • EEC
  • p53 family
  • p63

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

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