ArticleVirology2007
Characterization of the nuclear localization signal of high risk HPV16 E2 protein.
Article in Virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Review
- Cottontail Rabbit Papillomavirus E1 and E2 Proteins Mutually Influence Their Subcellular Localizations.Journal of virology · 2018Article
- Kinase Activity of Fibroblast Growth Factor Receptor 3 Regulates Activity of the Papillomavirus E2 Protein.Journal of virology · 2017Article
- Article
- Brd4-mediated nuclear retention of the papillomavirus E2 protein contributes to its stabilization in host cells.Viruses · 2014Article
- The papillomavirus E2 proteins.Virology · 2013Review
- Common importin alpha specificity for papillomavirus E2 proteins.Virus research · 2010Article
- Identification of the nuclear localization and export signals of high risk HPV16 E7 oncoprotein.Virology · 2009Article
- Modification of papillomavirus E2 proteins by the small ubiquitin-like modifier family members (SUMOs).Virology · 2008Article
- Comprehensive comparison of the interaction of the E2 master regulator with its cognate target DNA sites in 73 human papillomavirus types by sequence statistics.Nucleic acids research · 2008Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
The E2 protein of high risk human papillomavirus type 16 (HPV16) contains an amino-terminal (N) domain, a hinge (H) region and a carboxyl-terminal (C) DNA-binding domain. Using enhanced green fluorescent protein (EGFP) fusions with full length E2 and E2 domains in transfection assays in HeLa cells, we found that the C domain is responsible for the nuclear localization of E2 in vivo, whereas the N and H domains do not contain additional nuclear localization signals (NLSs). Deletion analysis of EGFP-E2 and EGFP-cE2 determined that the C domain contains an alpha helix cNLS that overlaps with the DNA-binding region. Mutational analysis revealed that the arginine and lysine residues in this cNLS are essential for nuclear localization of HPV16 E2. Interestingly, these basic amino acid residues are well conserved among the E2 proteins of BPV-1 and some high risk HPV types but not in the low risk HPV types, suggesting that there are differences between the NLSs and corresponding nuclear import pathways between these E2 proteins.
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Registered trials
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