ArticleJournal of virology2007
PATJ, a tight junction-associated PDZ protein, is a novel degradation target of high-risk human papillomavirus E6 and the alternatively spliced isoform 18 E6.
Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
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Who cites it
47 citing papers in PubMed, 1 synthesis or guideline pooled it, 88 citations in OpenAlex.
- Transcriptome meta-analysis reveals a dysregulation in extra cellular matrix and cell junction associated gene signatures during Dengue virus infection.Scientific reports · 2016Pooled it
- HPV E6/E7: insights into their regulatory role and mechanism in signaling pathways in HPV-associated tumor.Cancer gene therapy · 2024Review
- Viral subversion of the cell polarity regulator Scribble.Biochemical Society transactions · 2023Review
- Convergent copy number increase of genes associated with freshwater colonization in fishes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2022Article
- Molecular insights into the interaction of HPV-16 E6 variants against MAGI-1 PDZ1 domain.Scientific reports · 2022Article
- Virus-associated disruption of mucosal epithelial tight junctions and its role in viral transmission and spread.Tissue barriers · 2021Review
- Human papillomavirus E6 and E7: What remains?Tumour virus research · 2021Review
- The human papillomavirus oncoproteins: a review of the host pathways targeted on the road to transformation.The Journal of general virology · 2021Review
- Viral PDZ Binding Motifs Influence Cell Behavior Through the Interaction with Cellular Proteins Containing PDZ Domains.Methods in molecular biology (Clifton, N.J.) · 2021Review
- Comparative RNA sequencing reveals that HPV16 E6 abrogates the effect of E6*I on ROS metabolism.Scientific reports · 2019Article
- Upsetting the Balance: When Viruses Manipulate Cell Polarity Control.Journal of molecular biology · 2018Review
- Human Papillomavirus E6 interaction with cellular PDZ domain proteins modulates YAP nuclear localization.Virology · 2018Article
- Review
- Roles of the PDZ-binding motif of HPV 16 E6 protein in oncogenic transformation of human cervical keratinocytes.Cancer science · 2017Article
- Comparative analysis of HPV16 gene expression profiles in cervical and in oropharyngeal squamous cell carcinoma.Oncotarget · 2017Article
- Mitotic control of human papillomavirus genome-containing cells is regulated by the function of the PDZ-binding motif of the E6 oncoprotein.Oncotarget · 2017Article
- HCV NS4B targets Scribble for proteasome-mediated degradation to facilitate cell transformation.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- A Drosophila Model of HPV E6-Induced Malignancy Reveals Essential Roles for Magi and the Insulin Receptor.PLoS pathogens · 2016Article
- KSHV-Mediated Regulation of Par3 and SNAIL Contributes to B-Cell Proliferation.PLoS pathogens · 2016Article
- Viral Interactions with PDZ Domain-Containing Proteins-An Oncogenic Trait?Pathogens (Basel, Switzerland) · 2016Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The E6 protein from high-risk human papillomavirus types interacts with and degrades several PDZ domain-containing proteins that localize to adherens junctions or tight junctions in polarized epithelial cells. We have identified the tight junction-associated multi-PDZ protein PATJ (PALS1-associated TJ protein) as a novel binding partner and degradation target of high-risk types 16 and 18 E6. PATJ functions in the assembly of the evolutionarily conserved CRB-PALS1-PATJ and Par6-aPKC-Par3 complexes and is critical for the formation of tight junctions in polarized cells. The ability of type 18 E6 full-length to bind to, and the subsequent degradation of, PATJ is dependent on its C-terminal PDZ binding motif. We demonstrate that the spliced 18 E6* protein, which lacks a C-terminal PDZ binding motif, associates with and degrades PATJ independently of full-length 18 E6. Thus, PATJ is the first binding partner that is degraded in response to both isoforms of 18 E6. The ability of E6 to utilize a non-E6AP ubiquitin ligase for the degradation of several PDZ binding partners has been suggested. We also demonstrate that 18 E6-mediated degradation of PATJ is not inhibited in cells where E6AP is silenced by shRNA. This suggests that the E6-E6AP complex is not required for the degradation of this protein target.
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