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Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53

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1994

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Huibregtse, Jon M.
Howley, Peter M.

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Proceedings of the National Academy of Sciences. 1994, 91(19), pp. 8797-8801. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.91.19.8797

Zusammenfassung

The E6 protein of the oncogenic human papillomavirus types 16 and 18 facilitates the rapid degradation of the tumor-suppressor protein p53 via the ubiquitin-dependent proteolytic pathway. The E6 protein binds to a cellular protein of 100 kDa termed E6-AP. The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2). This mammalian E2 activity could be replaced with bacterially expressed UBC8 from Arabidopsis thaliana, which belongs to a subfamily of E2s including yeast UBC4 and UBC5 which are highly conserved at the amino acid level. In this paper we describe the cloning of a human cDNA encoding a human E2 that we have designated UbcH5 and that is related to Arabidopsis UBC8 and the other members of this subfamily. We demonstrate that UbcH5 can function in the E6/E6-AP-induced ubiquitination of p53.

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570 Biowissenschaften, Biologie

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paplflomavirus; E6-assodated protein; tumor-suppressor protein

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ISO 690SCHEFFNER, Martin, Jon M. HUIBREGTSE, Peter M. HOWLEY, 1994. Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. In: Proceedings of the National Academy of Sciences. 1994, 91(19), pp. 8797-8801. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.91.19.8797
BibTex
@article{Scheffner1994Ident-42769,
  year={1994},
  doi={10.1073/pnas.91.19.8797},
  title={Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53},
  number={19},
  volume={91},
  issn={0027-8424},
  journal={Proceedings of the National Academy of Sciences},
  pages={8797--8801},
  author={Scheffner, Martin and Huibregtse, Jon M. and Howley, Peter M.}
}
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