The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Stabilization of HPV16 E6 protein by PDZ proteins, and potential implications for genome maintenance
Abstract
The E6 protein from high-risk human papillomaviruses appears necessary for persistence of viral episomes in cells but the underlying mechanism is unclear. E6 has many activities, including its ability to bind and degrade PDZ domain-containing proteins, such as hScrib. However little is known about the role of these interactions for E6 function and the viral life cycle. We now show that the levels of expression of wild-type E6 are increased in the presence of hScrib whilst a mutant E6 protein lacking the PDZ-binding motif is found at lower levels as it is turned over more rapidly by the proteasome. This correlates with an inability of genomes containing this mutation to be maintained as episomes. These results show that E6 association with certain PDZ domain-containing proteins can stabilize the levels of E6 expression and provides one explanation as to how the PDZ-binding capacity of E6 might contribute to genome episomal maintenance.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“viruses defective in binding to polarity proteins are dampened in their ability to produce viral progeny and have deregulated viral genome maintenance, leading to a higher likelihood of the genome integrating into host DNA [283,284,285], thereby inducing deregulated expression of HPV oncoproteins and their carcinogenic orchestrations.”
From The Not-So-Good, the Bad and the Ugly: HPV E5, E6 and E7 Oncoproteins in the Orchestration of Carcinogenesis (2021) · cites this paper as [285]
Citations
Cites
Molecular biology of human papillomavirus infection and cervical cancer
Doorbar, J. (2006) · Clinical Science · doi:10.1042/cs20050369 · Cited by 1,072
Self-citationHuibregtse, J. M., Scheffner, M., & Howley, P. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb04990.x · Cited by 879
Nominé, Y., Masson, M., Charbonnier, S., Zanier, K., Ristriani, T., Deryckère, F., Sibler, A.-P., Desplancq, D., Atkinson, R. A., Weiss, E., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.024 · Cited by 177
The cell polarity regulator hScrib controls ERK activation through a KIM site-dependent interaction
Nagasaka, K., Pim, D., Massimi, P., Thomas, M., Tomaić, V, Subbaiah, V. K., Kranjec, C., Nakagawa, S., Yano, T., Taketani, Y., et al. (2010) · Oncogene · doi:10.1038/onc.2010.265 · Cited by 75
Self-citation
Research works printed but not linked: 39
- Allen-Hoffmann, 2000, Normal growth and differentiation in a spontaneously immortalized near-diploid human keratinocyte cell line, NIKS, J. Invest. Dermatol., 114, 444, 10.1046/j.1523-1747.2000.00869.x · DOI
- Charbonnier, 2011, The structural and dynamic response of MAGI-1 PDZ1 with noncanonical domain boundaries to the binding of human papillomavirus E6, J. Mol. Biol., 406, 745, 10.1016/j.jmb.2011.01.015 · DOI
- Forrester, 1992, Construction and properties of a mutant of herpes simplex virus type 1 with glycoprotein H coding sequences deleted, J. Virol., 66, 341, 10.1128/jvi.66.1.341-348.1992 · DOI
- Foster, 1994, The ability of human papillomavirus E6 proteins to target p53 for degradation in vivo correlates with their ability to abrogate actinomycin D-induced growth arrest, J. Virol., 68, 5698, 10.1128/jvi.68.9.5698-5705.1994 · DOI · Paper page
- Gardiol, 1999, Oncogenic human papillomavirus E6 proteins target the discs large tumour suppressor for proteasome-mediated degradation, Oncogene, 18, 5487, 10.1038/sj.onc.1202920 · DOI · Paper page
- Glaunsinger, 2000, Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins, Oncogene, 19, 5270, 10.1038/sj.onc.1203906 · DOI · Paper page
- Hoffmann, 2006, Different modes of human papillomavirus DNA replication during maintenance, J. Virol., 80, 4431, 10.1128/JVI.80.9.4431-4439.2006 · DOI
- Howley, 2001, Papillomaviruses and Their Replication, Vol. 2, 2197
- Kao, 2000, Human papillomavirus type 16 E6 induces self-ubiquitination of the E6AP ubiquitin-protein ligase, J. Virol., 74, 6408, 10.1128/JVI.74.14.6408-6417.2000 · DOI
- Kehmeier, 2002, Cellular steady-state levels of “high risk” but not “low risk” human papillomavirus (HPV) E6 proteins are increased by inhibition of proteasome-dependent degradation independent of their p53- and E6AP-binding capabilities, Virology, 299, 72, 10.1006/viro.2002.1502 · DOI
- Kiyono, 1997, Binding of high-risk human papillomavirus E6 oncoproteins to the human homologue of the Drosophila discs large tumor suppressor protein, Proc. Natl Acad. Sci. U.S.A., 94, 11612, 10.1073/pnas.94.21.11612 · DOI · Paper page
- Lambert, 2005, Using an immortalized cell line to study the HPV life cycle in organotypic “raft” cultures, Meth. Mol. Med., 119, 141
- Latorre, 2005, Viral oncoprotein-induced mislocalization of select PDZ proteins disrupts tight junctions and causes polarity defects in epithelial cells, J. Cell Sci., 118, 4283, 10.1242/jcs.02560 · DOI
- Laurson, 2010, Epigenetic repression of E-cadherin by human papillomavirus 16 E7 protein, Carcinogenesis, 31, 918, 10.1093/carcin/bgq027 · DOI
- Lee, 2004, Role of the PDZ domain-binding motif of the oncoprotein E6 in the pathogenesis of human papillomavirus type 31, J. Virol., 78, 12366, 10.1128/JVI.78.22.12366-12377.2004 · DOI · Paper page
- Lee, 2007, Analysis of the roles of E6 binding to E6TP1 and nuclear localization in the human papillomavirus type 31 life cycle, Virology, 358, 201, 10.1016/j.virol.2006.08.028 · DOI
- Lepik, 1998, p53 Protein is a suppressor of papillomavirus DNA amplificational replication, J. Virol., 72, 6822, 10.1128/JVI.72.8.6822-6831.1998 · DOI
- Liu, 2005, The E6AP ubiquitin ligase is required for transactivation of the hTERT promoter by the human papillomavirus E6 oncoprotein, J. Biol. Chem., 280, 10807, 10.1074/jbc.M410343200 · DOI · Paper page
- Massimi, 2004, HPV E6 specifically targets different cellular pools of its PDZ domain-containing tumour suppressor substrates for proteasome-mediated degradation, Oncogene, 23, 8033, 10.1038/sj.onc.1207977 · DOI
- Massimi, 2006, Phosphorylation of the discs large tumour suppressor protein controls its membrane localisation and enhances its susceptibility to HPV E6-induced degradation, Oncogene, 25, 4276, 10.1038/sj.onc.1209457 · DOI
- McIntosh, 2008, Structural analysis reveals an amyloid form of the human papillomavirus type 16 E1–E4 protein and provides a molecular basis for its accumulation, J. Virol., 82, 8196, 10.1128/JVI.00509-08 · DOI
- Nagasaka, 2006, Human homolog of Drosophila tumor suppressor Scribble negatively regulates cell-cycle progression from G1 to S phase by localizing at the basolateral membrane in epithelial cells, Cancer Sci., 97, 1217, 10.1111/j.1349-7006.2006.00315.x · DOI
- Nakagawa, 2000, Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase, Mol. Cell. Biol., 20, 8244, 10.1128/MCB.20.21.8244-8253.2000 · DOI · Paper page
- Narayan, 2009, The high-risk HPV E6 oncoprotein preferentially targets phosphorylated nuclear forms of hDlg, Virology, 387, 1, 10.1016/j.virol.2009.02.030 · DOI
- Nguyen, 2003, The PDZ ligand domain of the human papillomavirus type 16 E6 protein is required for E6's induction of epithelial hyperplasia in vivo, J. Virol., 77, 6957, 10.1128/JVI.77.12.6957-6964.2003 · DOI
- Oh, 2004, Roles of the E6 and E7 proteins in the life cycle of low-risk human papillomavirus type 11, J. Virol., 78, 2620, 10.1128/JVI.78.5.2620-2626.2004 · DOI
- Park, 2002, Genetic analysis of high-risk e6 in episomal maintenance of human papillomavirus genomes in primary human keratinocytes, J. Virol., 76, 11359, 10.1128/JVI.76.22.11359-11364.2002 · DOI
- Pim, 2010, Interaction of viral oncoproteins with cellular target molecules: infection with high-risk vs low-risk human papillomaviruses, APMIS, 118, 471, 10.1111/j.1600-0463.2010.02618.x · DOI
- Scheffner, 1990, The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53, Cell, 63, 1129, 10.1016/0092-8674(90)90409-8 · DOI · Paper page
- Stewart, 2004, Ubiquitination and proteasome degradation of the E6 proteins of human papillomavirus types 11 and 18, J. Gen. Virol., 85, 1419, 10.1099/vir.0.19679-0 · DOI
- Taylor, 2003, A novel technique with enhanced detection and quantitation of HPV-16 E1- and E2-mediated DNA replication, Virology, 315, 103, 10.1016/S0042-6822(03)00588-9 · DOI
- Thomas, 1999, Human papillomavirus type 31 oncoproteins E6 and E7 are required for the maintenance of episomes during the viral life cycle in normal human keratinocytes, Proc. Natl Acad. Sci. U.S.A., 96, 8449, 10.1073/pnas.96.15.8449 · DOI
- Thomas, 2001, HPV E6 and MAGUK protein interactions: determination of the molecular basis for specific protein recognition and degradation, Oncogene, 20, 5431, 10.1038/sj.onc.1204719 · DOI
- Thomas, 2005, The hScrib/Dlg apico-basal control complex is differentially targeted by HPV-16 and HPV-18 E6 proteins, Oncogene, 24, 6222, 10.1038/sj.onc.1208757 · DOI · Paper page
- Thomas, 2008, Human papillomaviruses, cervical cancer and cell polarity, Oncogene, 27, 7018, 10.1038/onc.2008.351 · DOI · Paper page
- Tomaic, 2009, The stability of the human papillomavirus E6 oncoprotein is E6AP dependent, Virology, 393, 7, 10.1016/j.virol.2009.07.029 · DOI · Paper page
- Walboomers, 1999, Human papillomavirus is a necessary cause of invasive cervical cancer worldwide, J. Pathol., 189, 12, 10.1002/(SICI)1096-9896(199909)189:1<12::AID-PATH431>3.0.CO;2-F · DOI
- Wang, 2009, Robust production and passaging of infectious HPV in squamous epithelium of primary human keratinocytes, Genes Dev., 23, 181, 10.1101/gad.1735109 · DOI
- Zhang, 2007, Structures of a human papillomavirus (HPV) E6 polypeptide bound to MAGUK proteins: mechanisms of targeting tumor suppressors by a high-risk HPV oncoprotein, J. Virol., 81, 3618, 10.1128/JVI.02044-06 · DOI
Cited by
Basukala, O., & Banks, L. (2021) · Viruses · doi:10.3390/v13101892 · Cited by 137
Self-citationAllosteric Conformational Barcodes Direct Signaling in the Cell
Nussinov, R., Ma, B., Tsai, C.-J., & Csermely, P. (2013) · Structure · doi:10.1016/j.str.2013.06.002 · Cited by 55
Metadata
- Authors
- Nicolaides, L., Davy, C., Raj, K., Kranjec, C., Banks, L., & Doorbar, J.
- Venue
- Virology
- Publisher
- Elsevier BV
- Published
- 2011-06
- Volume
- 414
- Issue
- 2
- Pages
- 137-145
- ISSN
- 0042-6822
- Cited by
- 53
- References
- 4
- Language
- en
- Licence
- Funders
- United Kingdom Medical Research Council (U117584278, U117573807)
- Associazione Italiana per la Ricerca sul Cancro
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Stabilization of HPV16 E6 protein by PDZ proteins, and potential implications for genome maintenance. https://app.cochat.ai/papers/10.1016/j.virol.2011.03.017
- The paper
- Nicolaides, L., Davy, C., Raj, K., Kranjec, C., Banks, L., & Doorbar, J. (2011). Stabilization of HPV16 E6 protein by PDZ proteins, and potential implications for genome maintenance. Virology. https://doi.org/10.1016/j.virol.2011.03.017