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A CELLULAR PROTEIN MEDIATES ASSOCIATION OF P53 WITH THE E6 ONCOPROTEIN OF HUMAN PAPILLOMAVIRUS TYPE-16 OR TYPE-18
Author(s): HUIBREGTSE JM, SCHEFFNER M, HOWLEY PM
Source: EMBO JOURNAL    Volume: 10    Issue: 13    Pages: 4129-4135    Published: DEC 1991  
Times Cited: 407     References: 48     
Abstract: The E6 protein of human papillomavirus types 16 and 18 (HPV-16 and HPV-18) can stably associate with the p53 protein in vitro. In the presence of rabbit reticulocyte lysate, this association leads to the specific degradation of p53 through the ubiquitin-dependent proteolysis system. We have examined the E6-p53 complex in more detail and have found that association of E6 with p53 is mediated by an additional cellular factor. This factor is present in rabbit reticulocyte lysate, primary human keratinocytes and in each of five human cell lines examined. The factor is designated E6-AP, for E6-associated protein, based on the observation that the E6 proteins of HPV-16 and 18 can form a stable complex with the factor in the absence of p53, whereas p53 association with the factor can be detected only in the presence of E6. Gel filtration and coprecipitation experiments indicate that E6-AP is a monomeric protein of approximately 100 kDa.
Document Type: Article
Language: English
Reprint Address: HUIBREGTSE, JM (reprint author), NCI, TUMOR VIRUS BIOL LAB, BETHESDA, MD 20892 USA
Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: GU645
ISSN: 0261-4189
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