ArticleJournal of virology2003
Hepatitis B virus X protein and simian virus 5 V protein exhibit similar UV-DDB1 binding properties to mediate distinct activities.
Article in Journal of virology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Screening of the HBx transactivation domain interacting proteins and the function of interactor Pin1 in HBV replication.Scientific reports · 2021Article
- Application of fluorescent-based technology detecting protein-protein interactions to monitor the binding of hepatitis B virus X protein to DNA-damage-binding protein 1.Biophysics and physicobiology · 2021Article
- Article
- The Antiresection Activity of the X Protein Encoded by Hepatitis Virus B.Hepatology (Baltimore, Md.) · 2019Article
- Breaking Bad: How Viruses Subvert the Cell Cycle.Frontiers in cellular and infection microbiology · 2018Review
- A Mass Spectrometry-Based Profiling of Interactomes of Viral DDB1- and Cullin Ubiquitin Ligase-Binding Proteins Reveals NF-κB Inhibitory Activity of the HIV-2-Encoded Vpx.Frontiers in immunology · 2018Article
- Identifying and Characterizing Interplay between Hepatitis B Virus X Protein and Smc5/6.Viruses · 2017Review
- DDB1 Stimulates Viral Transcription of Hepatitis B Virus via HBx-Independent Mechanisms.Journal of virology · 2016Article
- Article
- Hepatitis B virus X protein identifies the Smc5/6 complex as a host restriction factor.Nature · 2016Article
- Molecular biology of hepatitis B virus infection.Virology · 2015Review
- PCalign: a method to quantify physicochemical similarity of protein-protein interfaces.BMC bioinformatics · 2015Article
- The G1 phase E3 ubiquitin ligase TRUSS that gets deregulated in human cancers is a novel substrate of the S-phase E3 ubiquitin ligase Skp2.Cell cycle (Georgetown, Tex.) · 2015Article
- Detecting differential protein expression in large-scale population proteomics.Bioinformatics (Oxford, England) · 2014Article
- Interactions with DCAF1 and DDB1 in the CRL4 E3 ubiquitin ligase are required for Vpr-mediated G2 arrest.Virology journal · 2014Article
- Article
- Lentivirus Vpr and Vpx accessory proteins usurp the cullin4-DDB1 (DCAF1) E3 ubiquitin ligase.Current opinion in virology · 2012Review
- Hepatitis B virus X protein impedes the DNA repair via its association with transcription factor, TFIIH.BMC microbiology · 2011Article
- A promiscuous alpha-helical motif anchors viral hijackers and substrate receptors to the CUL4-DDB1 ubiquitin ligase machinery.Nature structural & molecular biology · 2010Article
- CRL4s: the CUL4-RING E3 ubiquitin ligases.Trends in biochemical sciences · 2009Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The UV-damaged DNA-binding activity protein (UV-DDB) consists of two subunits, DDB1 and DDB2, and functions in DNA repair and cell cycle regulation. The DDB1 subunit is a target for the hepatitis B virus X protein (HBx). Binding of HBx to DDB1 interferes with cell growth and viability in culture and has been implicated in the establishment of viral infection. DDB1 also interacts with the V proteins encoded by several paramyxoviruses including simian virus 5 (SV5), which prevent interferon signaling by targeting either STAT1 or STAT2 proteins for proteolysis. The role of V binding to DDB1, however, remains unclear. Here we show that the V protein of SV5 (SV5-V) and HBx exhibit strikingly similar DDB1 binding properties. Thus, SV5-V and HBx bind to DDB1 in a mutually exclusive manner, and SV5-V shares with HBx the ability to enhance the steady-state levels of DDB1 and to inhibit its association with DDB2. Yet only HBx induces cell death, and SV5-V can prevent HBx from doing so by blocking its interaction with DDB1. Binding of SV5-V to DDB1 may serve another function, since SV5-V shows a decreased ability to induce STAT1 degradation in cells expressing reduced amounts of DDB1. These findings demonstrate that HBx performs a unique function through its association with DDB1 for which SV5-V cannot substitute and suggest that SV5-V and HBx have evolved to bind DDB1 to achieve distinct functions, both by a mechanism that does not involve DDB2.
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