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Journal of Virology, June 2008, p. 5962-5966, Vol. 82, No. 12
0022-538X/08/$08.00+0     doi:10.1128/JVI.02747-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Transformation by Bovine Papillomavirus Type 1 E6 Requires Paxillin{triangledown}

Ramon Wade, Nicole Brimer, and Scott Vande Pol*

Department of Pathology, University of Virginia, P.O. Box 800904, Charlottesville, Virginia 22908-0904

Received 27 December 2007/ Accepted 26 March 2008

Papillomavirus E6 proteins are adapters that change the function of cellular regulatory proteins. The bovine papillomavirus type 1 E6 (BE6) binds to LXXLL peptide sequences termed LD motifs (consensus sequence LDXLLXXL) on the cellular protein paxillin that is a substrate of Src and focal adhesion kinases. Anchorage-independent transformation induced by BE6 required both paxillin and BE6-binding LD motifs on paxillin but was independent of the major tyrosine phosphorylation sites of paxillin. The essential role of paxillin in transformation by BE6 highlights the role of paxillin in the transduction of cellular signals that result in anchorage-independent cell proliferation.

* Corresponding author. Mailing address: Department of Pathology, University of Virginia, P.O. Box 800904, Charlottesville, VA 22908-0904. Phone: (434) 924-1603. Fax: (434) 924-2151. E-mail: vandepol{at}virginia.edu

{triangledown} Published ahead of print on 2 April 2008.

Journal of Virology, June 2008, p. 5962-5966, Vol. 82, No. 12
0022-538X/08/$08.00+0     doi:10.1128/JVI.02747-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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