Publikation: Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53
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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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SCHEFFNER, 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.91.19.8797BibTex
@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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