Interaction-of the human papillomavirus type 16 E6 oncoprotein with wild- type and mutant human p53 proteins

Martin Scheffner, Takashi Takahashi, Jon M. Huibregtse, John D. Minna, Peter M. Howley

Research output: Contribution to journalComment/debatepeer-review

118 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5100-5105
Number of pages6
JournalJournal of virology
Volume66
Issue number8
DOIs
StatePublished - 1992

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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