Publikation: Interaction of the human papillomavirus type 16 E6 oncoprotein with wild-type and mutant human p53 proteins
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The E6 oncoproteins encoded by the cancer-associated human papillomaviruses (HPVs) can associate with and promote the degradation of wild-type p53 in vitro. To gain further insight into this process, the ability of HPV-16 E6 to complex with and promote the degradation of mutant forms of p53 was studied. A correlation between binding and the targeted degradation of p53 was established. Mutant p53 proteins that bound HPV-16 E6 were targeted for degradation, whereas those that did not complex HPV-16 E6 were not degraded. Since the HPV-16 E6-promoted degradation involves the ubiquitin-dependent proteolysis pathway, specific mutations were made in the amino terminus of p53 to examine whether the E6 targeted degradation involved the N-end rule pathway. No requirement for destabilizing amino acids at the N terminus of p53 was found, nor was evidence found that HPV-16 E6 could provide this determinant in trans, indicating that the N-terminal rule pathway is not involved in the E6-promoted degradation of p53.
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SCHEFFNER, Martin, Takashi TAKAHASHI, Jon M. HUIBREGTSE, John D. MINNA, Peter M. HOWLEY, 1992. Interaction of the human papillomavirus type 16 E6 oncoprotein with wild-type and mutant human p53 proteins. In: Journal of Virology. 1992, 66(8), pp. 5100-5105. ISSN 0022-538X. eISSN 1098-5514BibTex
@article{Scheffner1992Inter-42701, year={1992}, title={Interaction of the human papillomavirus type 16 E6 oncoprotein with wild-type and mutant human p53 proteins}, url={http://jvi.asm.org/content/66/8/5100.abstract}, number={8}, volume={66}, issn={0022-538X}, journal={Journal of Virology}, pages={5100--5105}, author={Scheffner, Martin and Takahashi, Takashi and Huibregtse, Jon M. and Minna, John D. and Howley, Peter M.} }
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