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    Science. 1995 Jul 28;269(5223):529-31.

    Interaction of papillomavirus E6 oncoproteins with a putative calcium-binding protein.

    Chen JJ, Reid CE, Band V, Androphy EJ.

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    Department of Dermatology, New England Medical Center, Boston, MA, USA.

    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.

    PMID:
    7624774
    [PubMed - indexed for MEDLINE]

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