Interaction of zyxin, a focal adhesion protein, with the e6 protein from human papillomavirus type 6 results in its nuclear translocation.

Abstract:

: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 ((6)E6) and zyxin results in the accumulation of zyxin in the nucleus where it can function as a transcriptional activator. (6)E6 can also mobilize endogenous zyxin to the nucleus.

journal_name

J Virol

journal_title

Journal of virology

authors

Degenhardt YY,Silverstein S

doi

10.1128/JVI.75.23.11791-11802.2001

subject

Has Abstract

pub_date

2001-12-01 00:00:00

pages

11791-802

issue

23

eissn

0022-538X

issn

1098-5514

journal_volume

75

pub_type

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