Association of Bovine Papillomavirus Type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif (original) (raw)

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• Published: 21 January 1998

Oncogene volume 16, pages 43–52 (1998)Cite this article

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Abstract

We have found that the E6 oncoprotein of Bovine Papillomavirus Type 1 (BE6) as well as the E6 protein of the cancer associated HPV-16 (16E6) interact with the focal adhesion protein paxillin. Mutational analysis of paxillin revealed that BE6 binds paxillin through small protein interaction motifs called LD motifs that have been previously identified as important in regulating association of paxillin with vinculin and focal adhesion kinase (FAK), and that BE6 can interact with at least two separate binding sites on paxillin. The LD motifs of paxillin that bind BE6 share homology with the E6 binding site of E6-AP, a ubiquitin ligase that together with 16E6 targets the degradation of the p53 tumor suppressor. Paxillin binding to BE6 excludes simultaneous binding to E6-AP. Mutational analysis of BE6 can distinguish the interaction of BE6 with E6-AP compared to paxillin and revealed that the interaction of BE6 with paxillin may be necessary for the induction of anchorage independent growth of cells by BE6.

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Authors and Affiliations

1. Case Western Reserve University School of Medicine, Institute of Pathology, State University of New York at Syracuse, USA
   Scott B Vande Pol
2. Department of Anatomy and Cell Biology, State University of New York at Syracuse, USA
   Michael C Brown & Christopher E Turner

Authors

1. Scott B Vande Pol
2. Michael C Brown
3. Christopher E Turner

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Pol, S., Brown, M. & Turner, C. Association of Bovine Papillomavirus Type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif.Oncogene 16, 43–52 (1998). https://doi.org/10.1038/sj.onc.1201504

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• Received: 08 May 1997
• Revised: 15 August 1997
• Accepted: 15 August 1997
• Published: 21 January 1998
• Issue date: 08 January 1998
• DOI: https://doi.org/10.1038/sj.onc.1201504

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