Publikation: Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins
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E6-AP is a 100-kDa cellular protein that mediates the interaction of the human papillomavirus type 16 and 18 E6 proteins with p53. The association of p53 with E6 and E6-AP promotes the specific ubiquitination and subsequent proteolytic degradation of p53 in vitro. We recently isolated a cDNA encoding E6-AP and have now mapped functional domains of E6-AP involved in binding E6, association with p53, and ubiquitination of p53. The E6 binding domain consists of an 18-amino-acid region within the central portion of the molecule. Deletion of these 18 amino acids from E6-AP results in loss of both E6 and p53 binding activities. The region that directs p53 binding spans the E6 binding domain and consists of approximately 500 amino acids. E6-AP sequences in addition to those required for formation of a stable ternary complex with E6 and p53 are necessary to stimulate the ubiquitination of p53. These sequences lie within the C-terminal 84 amino acids of E6-AP. The entire region required for E6-dependent ubiquitination of p53 is also required for the ubiquitination of an artificial E6 fusion protein.
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HUIBREGTSE, Jon M., Martin SCHEFFNER, Peter M. HOWLEY, 1993. Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins. In: Molecular and Cellular Biology. 1993, 13(8), pp. 4918-4927. ISSN 0270-7306. eISSN 1098-5549. Available under: doi: 10.1128/MCB.13.8.4918BibTex
@article{Huibregtse1993Local-42703, year={1993}, doi={10.1128/MCB.13.8.4918}, title={Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins}, number={8}, volume={13}, issn={0270-7306}, journal={Molecular and Cellular Biology}, pages={4918--4927}, author={Huibregtse, Jon M. and Scheffner, Martin and Howley, Peter M.} }
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