Dual-site interactions of p53 protein transactivation domain with anti-apoptotic bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways

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Title
Dual-site interactions of p53 protein transactivation domain with anti-apoptotic bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways
Author(s)
Ji Hyang Ha; J S Shin; Mi Kyung Yoon; M S Lee; F He; Kwang-Hee Bae; H S Yoon; C K Lee; Sung Goo Park; Y Muto; Seung-Wook Chi
Bibliographic Citation
Journal of Biological Chemistry, vol. 288, no. 10, pp. 7387-7398
Publication Year
2013
Abstract
Background: Interactions between p53 and Bcl-2 family proteins serve a critical role in transcription-independent p53 apoptosis. Results: We studied the interactions of p53TAD2 with anti-apoptotic Bcl-2 family proteins at the atomic level by NMR, mutagenesis, and structure calculation. Conclusion: Bcl-XL/Bcl-2, MDM2, and CBP/p300 share similar modes of binding to the dual p53TAD motifs. Significance: Dual-site interaction of p53TAD is a highly conserved mechanism in the transcription-dependent and transcription- independent p53 apoptotic pathways.
ISSN
0021-9258
Publisher
Amer Soc Biochemistry Molecular Biology Inc
DOI
http://dx.doi.org/10.1074/jbc.M112.400754
Type
Article
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Biomedical Research > 1. Journal Articles
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