14-3-3 activation of DNA binding of p53 by enhancing its association into tetramers

• Published in: Nucleic acids research Vol. 36; no. 18; pp. 5983 - 5991
• Main Authors: Rajagopalan, Sridharan, Jaulent, Agnes M, Wells, Mark, Veprintsev, Dmitry B, Fersht, Alan R
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.10.2008; Oxford Publishing Limited (England)
• Subjects: 14-3-3 Proteins - chemistry; 14-3-3 Proteins - metabolism; acetylation; Base Sequence; Binding Sites; Deoxyribonucleic acid; dissociation; DNA; DNA - chemistry; DNA - metabolism; DNA damage; Fluorescence Polarization; Molecular Biology; neoplasms; Peptides; Peptides - metabolism; Phosphopeptides - metabolism; Phosphorylation; post-translational modification; Protein Binding; Protein Structure, Tertiary; proteins; serine; Tumor Suppressor Protein p53 - chemistry; Tumor Suppressor Protein p53 - metabolism; ultracentrifugation
• ISSN: 0305-1048; 1362-4962; 1362-4962
• DOI: 10.1093/nar/gkn598

Activation of the tumour suppressor p53 on DNA damage involves post-translational modification by phosphorylation and acetylation. Phosphorylation of certain residues is critical for p53 stabilization and plays an important role in DNA-binding activity. The 14-3-3 family of proteins activates the DN...