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Journal of Virology, September 2009, p. 8885-8892, Vol. 83, No. 17
0022-538X/09/$08.00+0     doi:10.1128/JVI.00605-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

The Ubiquitin-Specific Peptidase USP15 Regulates Human Papillomavirus Type 16 E6 Protein Stability{triangledown} ,§

Robin M. Vos, Jennifer Altreuter, Elizabeth A. White, and Peter M. Howley*

Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115

Received 24 March 2009/ Accepted 18 June 2009

Proteomic identification of human papillomavirus type 16 (HPV16) E6-interacting proteins revealed several proteins involved in ubiquitin-mediated proteolysis. In addition to the well-characterized E6AP ubiquitin-protein ligase, a second HECT domain protein (HERC2) and a deubiquitylating enzyme (USP15) were identified by tandem affinity purification of HPV16 E6-associated proteins. This study focuses on the functional consequences of the interaction of E6 with USP15. Overexpression of USP15 resulted in increased levels of the E6 protein, and the small interfering RNA-mediated knockdown of USP15 decreased E6 protein levels. These results implicate USP15 directly in the regulation of E6 protein stability and suggest that ubiquitylated E6 could be a substrate for USP15 ubiquitin peptidase activity. It remains possible that E6 could affect the activity of USP15 on specific cellular substrates, a hypothesis that can be tested as more is learned about the substrates and pathways controlled by USP15.

* Corresponding author. Mailing address: 77 Avenue Louis Pasteur, New Research Building Room 950, Department of Pathology, Harvard Medical School, Boston, MA 02115. Phone: (617) 432-2884. Fax: (617) 432-2882. E-mail: peter_howley{at}hms.harvard.edu

{triangledown} Published ahead of print on 24 June 2009.

§ Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, September 2009, p. 8885-8892, Vol. 83, No. 17
0022-538X/09/$08.00+0     doi:10.1128/JVI.00605-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Liu, X., Dakic, A., Zhang, Y., Dai, Y., Chen, R., Schlegel, R. (2009). HPV E6 protein interacts physically and functionally with the cellular telomerase complex. Proc. Natl. Acad. Sci. USA 106: 18780-18785 [Abstract] [Full Text]  


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