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Published on: July 23, 2010
Peptide interactions stabilize and restructure human papillomavirus type 16 E6 to interact with p53
Tina Ansari1, Nicole Brimer, Scott B Vande Pol
1Department of Pathology, University of Virginia, Charlottesville, Virginia, USA.
Journal of Virology
|August 17, 2012
Summary
Human papillomavirus type 16 E6 protein (16E6) interacts with p53, targeting it for degradation. Minimal 16E6-binding peptides stabilize 16E6 and enable p53 interaction, but E6AP is essential for p53 degradation.
Area of Science:
- Oncology
- Virology
- Molecular Biology
Background:
- Human papillomavirus type 16 E6 (HPV-16 16E6) targets the tumor suppressor p53 for degradation.
- HPV-16 16E6 interacts with p53 via the E3 ubiquitin ligase E6AP.
Purpose of the Study:
- To investigate the mechanism by which HPV-16 16E6 reshapes to bind p53.
- To elucidate the role of LXXLL peptides in 16E6 function and p53 degradation.
Main Methods:
- Utilized minimal 16E6-binding LXXLL peptides.
- Assessed 16E6 interaction with p53 in vivo.
- Evaluated the requirement of E6AP expression for p53 degradation.
Main Results:
- Minimal 16E6-binding LXXLL peptides reshape 16E6, enabling p53 interaction and in vivo stabilization.
- Degradation of p53 by 16E6 is dependent on E6AP expression.
Conclusions:
- Papillomavirus E6 proteins utilize LXXLL peptides as a general mechanism to reshape E6 into an adapter molecule.
- This reshaping facilitates interaction with cellular targets like p53, with E6AP being crucial for downstream degradation pathways.
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