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Bovine papillomavirus E5 oncoprotein binds to the 16K component of vacuolar H+-ATPases

Nature volume 352, pages 347–349 (1991)Cite this article

Abstract

THE major transforming protein of bovine papillomavirus type 1, á£5 (refs 1–4), is mainly associated with endomembranes5, 6, specifically binding to a cellular protein of relative molecular mass 16,000 (16K) (ref. 7). At the same time as transformation, E5 causes the phosphorylation of tyrosine residues in epidermal and platelet-derived growth factor receptors8, 9. We show here that the 16K protein associated with E5 is the 16K component of vacuolar ATPases. This protein is known to be an integral membrane protein in endosomes, bovine chromaffin granules, synaptic vesicles, fungal and plant vacuoles and clathrin-coated vesicles10–16, as well as a component of gap-junction-like membrane complexes17. Because proton pumps are critical for the function of cellular compartments that process growth-factor receptors, the interaction of E5 with the 16K protein could explain the pleiomorphic features of cells transformed by E5.

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Author notes

  1. Vivien Bubb

    Present address: Department of Pathology, University Medical School, University of Edinburgh, Teviot Place, Edinburgh, EH8 9AG, UK

Authors and Affiliations

  1. Department of Pathology, Georgetown University, Washington, DC 20007, USA

    David J. Goldstein, Thorkell Andresson, Vivien Bubb & Richard Schlegel

  2. Beatson Institute for Cancer Research, Garscube Estate, Switchback Road, Bearsden, Glasgow, G61 1BD, UK

    Malcolm E. Fmbow , Pauline McLean & Ken Smith

Authors
  1. David J. Goldstein
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  5. Ken Smith
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  6. Vivien Bubb
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  7. Richard Schlegel
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Goldstein, D., Fmbow , M., Andresson, T. et al. Bovine papillomavirus E5 oncoprotein binds to the 16K component of vacuolar H+-ATPases. Nature 352, 347–349 (1991). https://doi.org/10.1038/352347a0

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