iASPP preferentially binds p53 proline-rich region and modulates apoptotic function of codon 72-polymorphic p53.

Journal article

iASPP is one of the most evolutionarily conserved inhibitors of p53, whereas ASPP1 and ASPP2 are activators of p53. We show here that, in addition to the DNA-binding domain, the ASPP family members also bind to the proline-rich region of p53, which contains the most common p53 polymorphism at codon 72. Furthermore, the ASPP family members, particularly iASPP, bind to and regulate the activity of p53Pro72 more efficiently than that of p53Arg72. Hence, escape from negative regulation by iASPP i...

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Authors: Bergamaschi, D; Samuels, Y; Sullivan, A; Zvelebil, M; Breyssens, H

• Publication status: Published
• Journal: Nature genetics
• Volume: 38
• Issue: 10
• Pages: 1133-1141
• Publication date: 2006-10-01
• DOI: 10.1038/ng1879
• EISSN: 1546-1718
• ISSN: 1061-4036
• Language: English
• Keywords: Apoptosis; Tyrosine; Binding Sites; Homozygote; Conserved Sequence; Polymorphism, Genetic; Intracellular Signaling Peptides and Proteins; Tumor Suppressor Protein p53; Humans; Female; Repressor Proteins; Amino Acid Sequence; Molecular Sequence Data; Cells, Cultured; Breast Neoplasms; Gene Expression Regulation; Arginine; Codon; Proline; Carcinoma