Abstract
Human papillomaviruses (HPVs) are associated with the majority of cervical cancers and encode a transforming protein, E6, that interacts with the tumor suppressor protein p53. Because E6 has p53-independent transforming activity, the yeast two-hybrid system was used to search for other E6-binding proteins. One such protein, E6BP, interacted with cancer-associated HPV E6 and with bovine papillomavirus type 1 (BPV-1) E6. The transforming activity of BPV-1 E6 mutants correlated with their E6BP-binding ability. E6BP is identical to a putative calcium-binding protein, ERC-55, that appears to be localized in the endoplasmic reticulum.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Bovine papillomavirus 1 / physiology
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Calcium-Binding Proteins / analysis
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Calcium-Binding Proteins / metabolism*
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Cell Transformation, Viral
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Cells, Cultured
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Endoplasmic Reticulum / chemistry
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HeLa Cells
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Humans
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Oncogene Proteins, Viral / analysis
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Oncogene Proteins, Viral / metabolism*
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Papillomaviridae*
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Recombinant Fusion Proteins / metabolism
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Repressor Proteins*
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Ubiquitin-Protein Ligases
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Viral Proteins / metabolism
Substances
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Calcium-Binding Proteins
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E6 protein, Human papillomavirus type 16
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Oncogene Proteins, Viral
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RCN2 protein, human
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Recombinant Fusion Proteins
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Repressor Proteins
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Viral Proteins
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protein E6, Bovine papillomavirus
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Ubiquitin-Protein Ligases