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.

Lena, A.M., Duca, S., Novelli, F., Melino, S., Annicchiarico-Petruzzelli, M., Melino, G., et al. (2015). Amino-terminal residues of Δnp63, mutated in ectodermal dysplasia, are required for its transcriptional activity. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 467(2), 434-440 [10.1016/j.bbrc.2015.09.111].

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

LENA, ANNA MARIA;MELINO, SONIA MICHAELA;MELINO, GENNARO;CANDI, ELEONORA
2015-11

Abstract

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.
Pubblicato
Rilevanza internazionale
Articolo
Esperti anonimi
Settore BIO/10
Settore BIO/11
English
AEC; Ankyloblepharon-Ectodermal defects-cleft lip/palate syndrome; EEC; Ectodermal dysplasia; Ectrodactyly-Ectodermal dysplasia and cleft lip/palate syndrome; p53 family; p63; Binding Sites; Carrier Proteins; Cell Line, Tumor; Cyclin-Dependent Kinase Inhibitor p21; Cytoskeletal Proteins; Ectodermal Dysplasia; Genes, Reporter; HEK293 Cells; Humans; Keratin-14; Luciferases; Membrane Proteins; Molecular Sequence Data; Nerve Tissue Proteins; Open Reading Frames; Protein Binding; Protein Precursors; Protein Structure, Tertiary; Recombinant Proteins; Response Elements; Transcription Factors; Tumor Suppressor Proteins; Amino Acid Sequence; Sequence Deletion; Transcriptional Activation
Lena, A.M., Duca, S., Novelli, F., Melino, S., Annicchiarico-Petruzzelli, M., Melino, G., et al. (2015). Amino-terminal residues of Δnp63, mutated in ectodermal dysplasia, are required for its transcriptional activity. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 467(2), 434-440 [10.1016/j.bbrc.2015.09.111].
Lena, Am; Duca, S; Novelli, F; Melino, Sm; Annicchiarico Petruzzelli, M; Melino, G; Candi, E
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/152747
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