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Journal of Virology, December 2001, p. 11791-11802, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11791-11802.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Interaction of Zyxin, a Focal Adhesion Protein, with the E6 Protein from Human Papillomavirus Type 6 Results in Its Nuclear Translocation

Yan Yan Degenhardt1 and Saul Silverstein2,*

Departments of Pharmacology1 and Microbiology,2 College of Physicians and Surgeons, Columbia University, New York, New York 10032

Received 16 May 2001/Accepted 5 September 2001

Zyxin, a focal adhesion molecule, interacts specifically with the E6 protein from human papillomavirus (HPV) type 6 in a yeast two-hybrid screen of a cDNA library prepared from human keratinocytes. Zyxin does not interact significantly with E6 proteins from HPV types 11, 16, or 18. The interaction was confirmed by in vitro and in vivo analyses and it requires the LIM domains (Lin-11, Isl-1, and Mec-3 [G. Freyd, S. K. Kim, and H. R. Horvitz, Nature 344:876-879, 1990]) found at the carboxyl terminus of zyxin. Cotransfection of E6 from HPV (6E6) and zyxin results in the accumulation of zyxin in the nucleus where it can function as a transcriptional activator. 6E6 can also mobilize endogenous zyxin to the nucleus.

* Corresponding author. Mailing address: Department of Microbiology, College of Physicians and Surgeons, Columbia University, 701 W. 168th St., New York, NY 10032. Phone: (212) 305-8149. Fax: (212) 305-5106. E-mail: sjs6{at}columbia.edu.

Journal of Virology, December 2001, p. 11791-11802, Vol. 75, No. 23
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.23.11791-11802.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.