ArticleProceedings of the National Academy of Sciences of the United States of America2003
Replication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin-proteasome pathway.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 35 citations in OpenAlex.
- The herpes simplex origin-binding protein: mechanisms for sequence-specific DNA binding and dimerization revealed by Cryo-EM.Nucleic acids research · 2025Article
- Ubiquitination Regulates Reorganization of the Membrane System During Cytomegalovirus Infection.Life (Basel, Switzerland) · 2025Article
- Post-translational modifications as a key mechanism for herpes simplex virus type I evasion of host innate immunity.Frontiers in microbiology · 2025Review
- Host Cell Neddylation Facilitates Alphaherpesvirus Entry in a Virus-Specific and Cell-Dependent Manner.Microbiology spectrum · 2022Article
- Inhibition of herpes simplex virus-1 infection by MBZM-N-IBT: in silico and in vitro studies.Virology journal · 2021Article
- MG-132 reduces virus release in Bovine herpesvirus-1 infection.Scientific reports · 2017Article
- Replication and recombination of herpes simplex virus DNA.The Journal of biological chemistry · 2011Review
- Cellular proteasome activity facilitates herpes simplex virus entry at a postpenetration step.Journal of virology · 2008Article
- Direct interaction between the N- and C-terminal portions of the herpes simplex virus type 1 origin binding protein UL9 implies the formation of a head-to-tail dimer.Journal of virology · 2007Article
- Reduction of infectious bursal disease virus replication in cultured cells by proteasome inhibitors.Virus genes · 2007Article
- Cathepsin B mediates cleavage of herpes simplex virus type 1 origin binding protein (OBP) to yield OBPC-1, and cleavage is dependent upon viral DNA replication.Journal of virology · 2007Article
- DNA binding activity of the herpes simplex virus type 1 origin binding protein, UL9, can be modulated by sequences in the N terminus: correlation between transdominance and DNA binding.Journal of virology · 2006Article
- The cellular localization pattern of Varicella-Zoster virus ORF29p is influenced by proteasome-mediated degradation.Journal of virology · 2006Article
- Pyrrolidine dithiocarbamate reduces coxsackievirus B3 replication through inhibition of the ubiquitin-proteasome pathway.Journal of virology · 2005Article
- The neural F-box protein NFB42 mediates the nuclear export of the herpes simplex virus type 1 replication initiator protein (UL9 protein) after viral infection.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- Herpes simplex virus infections are arrested in Oct-1-deficient cells.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
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2 authors at 1 institution in 1 country.
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Abstract
The ubiquitin-proteasome pathway plays a critical role in the degradation of short-lived and regulatory proteins in a variety of cellular processes. The F-box proteins are part of the ubiquitin-ligase complexes, which mediate ubiquitination and proteasome-dependent degradation of phosphorylated proteins. We previously identified NFB42, an F-box protein that is highly enriched in the nervous system, as a binding partner for the herpes simplex virus 1 UL9 protein, the viral replication-initiator protein, in a yeast two-hybrid screen. In the present work, we find that coexpression of NFB42 and UL9 genes in 293T cells leads to a significant decrease in the level of UL9 protein. Treatment with the 26S-proteasome inhibitor MG132 restores the UL9 protein to normal levels. We have observed also that the UL9 protein is polyubiquitinated in vivo and that the interaction between NFB42 and the UL9 protein is dependent upon phosphorylation of the UL9 protein. These results suggest that the interaction of the UL9 protein with NFB42 results in its polyubiquitination and subsequent degradation by the 26S proteasome. They suggest further a mechanism by which latency of herpes simplex virus 1 can be established in neuronal cells.
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