The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.
A cellular protein mediates association of p53 with the E6 oncoprotein of human papillomavirus types 16 or 18.
Open accessAbstract
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.
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The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
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Self-citationThe human papilloma virus-16 E7-oncoprotein is able to bind to the retinoblastoma gene product
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Self-citationAssociation of Human Papillomavirus Types 16 and 18 E6 Proteins with p53
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Self-citationT antigen is bound to a host protein in SY40-transformed cells
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The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
Scheffner, M., Huibregtse, J. M., Vierstra, R. D., & Howley, P. M. (1993) · Cell · doi:10.1016/0092-8674(93)90384-3 · Cited by 2,416
Self-citationHuman papillomavirus oncoproteins: pathways to transformation
Moody, C. A., & Laimins, L. A. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2886 · Cited by 1,814
UBIQUITIN-DEPENDENT PROTEIN DEGRADATION
Hochstrasser, M. (1996) · Annual Review of Genetics · doi:10.1146/annurev.genet.30.1.405 · Cited by 1,706
Zhang, Y., Xiong, Y., & Yarbrough, W. G. (1998) · Cell · doi:10.1016/s0092-8674(00)81401-4 · Cited by 1,626
Protein ubiquitination involving an E1–E2–E3 enzyme ubiquitin thioester cascade
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Metadata
- Authors
- Huibregtse, J. M., Scheffner, M., & Howley, P. M.
- Affiliations
- National Institutes of Health (US)
- Venue
- The EMBO Journal
- Published
- 1991-12-01
- Volume
- 10
- Issue
- 13
- Pages
- 4129-4135
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC453163
- OpenAlex
- W140061535
- Cited by
- 879
- References
- 46
- Citations by year
- 2026: 8 · 2025: 15 · 2024: 16 · 2023: 26 · 2022: 21 · 2021: 25 · 2020: 27 · 2019: 18 · 2018: 28 · 2017: 29 · 2016: 19 · 2015: 26 · 2014: 29 · 2013: 28 · 2012: 41
- FWCI
- 5.96
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- National Cancer Institute
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Health Sciences › Medicine › Epidemiology › Cervical Cancer and HPV Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- p53, E6 oncoprotein, HPV16, HPV 18, UBE3A, ubiquitin-mediated proteolysis, p53 degradation, protein-protein interaction, keratinocytes, tumor suppressor
- MeSH terms
- Animals, Cell Line, Chromatography, Gel, DNA-Binding Proteins, Electrophoresis, Polyacrylamide Gel, Humans, Hydrolysis, Oncogene Proteins, Viral, Plasmids, Protein Binding, Proteins, Repressor Proteins, Reticulocytes, Tumor Suppressor Protein p53, Papillomaviridae
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