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.
Original language | English (US) |
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Pages (from-to) | 529-531 |
Number of pages | 3 |
Journal | Science |
Volume | 269 |
Issue number | 5223 |
DOIs | |
State | Published - 1995 |
Externally published | Yes |
ASJC Scopus subject areas
- General