Chen J J, Reid C E, Band V, Androphy E J
Department of Dermatology, New England Medical Center, Boston, MA, USA.
Science. 1995 Jul 28;269(5223):529-31. doi: 10.1126/science.7624774.
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.
人乳头瘤病毒（HPV）与大多数宫颈癌相关，并编码一种转化蛋白E6，该蛋白与肿瘤抑制蛋白p53相互作用。由于E6具有不依赖p53的转化活性，因此利用酵母双杂交系统寻找其他与E6结合的蛋白。其中一种这样的蛋白E6BP，与癌症相关的HPV E6以及1型牛乳头瘤病毒（BPV-1）E6相互作用。BPV-1 E6突变体的转化活性与其E6BP结合能力相关。E6BP与一种假定的钙结合蛋白ERC-55相同，该蛋白似乎定位于内质网。
