Format

Send to

Choose Destination
See comment in PubMed Commons below
Proc Natl Acad Sci U S A. 1997 Apr 29;94(9):4412-7.

The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton.

Author information

1
Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.

Abstract

The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) has been shown to transform cells through a p53-independent pathway, but its transforming mechanism is unknown. Here we demonstrate in vitro and in vivo interactions between BPV-1 E6 and the focal adhesion protein paxillin. The ability of BPV-1 E6 to complex with paxillin correlated with its ability to transform; E6 mutant proteins impaired in their transformation function also were impaired in their abilities to bind paxillin. E6 binding to paxillin also may contribute to the carcinogenic potential of the human papillomavirus (HPV); we were able to show in vitro binding of paxillin to the E6 proteins of the cancer-associated type HPV 16 but not of the nononcogenic types 6 and 11. The association of E6 with paxillin was affected by depolymerization of the actin fiber network, and overexpression of BPV-1 E6 led to disruption of actin fiber formation. Disruption of the actin cytoskeleton is a characteristic of many transformed cells, and, in BPV-1 transformed cells, may be mediated by BPV-1 E6 through its interaction with paxillin.

PMID:
9114003
PMCID:
PMC20736
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Support Center