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

The major transforming protein of bovine papillomavirus type 1, E5 (refs 1-4), is mainly associated with endomembranes, 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 i...

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Bibliographic Details
Published in:Nature (London) 1991-07, Vol.352 (6333), p.347-349
Main Authors: Goldstein, D.J, Finbow, M.E, Andresson, T, McLean, P, Smith, K, Bubb, V, Schlegel, R
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
adenosinetriphosphatase
amino acid sequences
Base Sequence
binding proteins
Biochemistry
Bovine papillomavirus
Bovine papillomavirus 1 - metabolism
Cells, Cultured
DNA-Binding Proteins - metabolism
Enzymes
Molecular Sequence Data
nucleotide sequences
Proteins
Vacuoles - metabolism
Viral Proteins - metabolism
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Summary:The major transforming protein of bovine papillomavirus type 1, E5 (refs 1-4), is mainly associated with endomembranes, 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 receptors. 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 vesicles, as well as a component of gap-junction-like membrane complexes. 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/352347a0