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Localization of the E6-AP regions that direct human papillomavirus E6 binding, association with p53, and ubiquitination of associated proteins

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1993

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Huibregtse, Jon M.
Howley, Peter M.

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Molecular and Cellular Biology. 1993, 13(8), pp. 4918-4927. ISSN 0270-7306. eISSN 1098-5549. Available under: doi: 10.1128/MCB.13.8.4918

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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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570 Biowissenschaften, Biologie

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ISO 690HUIBREGTSE, 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.13.8.4918
BibTex
@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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