ArticleProceedings of the National Academy of Sciences of the United States of America2001
The infected cell protein 0 of herpes simplex virus 1 dynamically interacts with proteasomes, binds and activates the cdc34 E2 ubiquitin-conjugating enzyme, and possesses in vitro E3 ubiquitin ligase activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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Who cites it
73 citing papers in PubMed, 117 citations in OpenAlex.
- Nuclear interferon-stimulated gene product maintains heterochromatin on the herpes simplex viral genome to limit lytic infection.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Regulation of Krüppel-Like Factor 15 Expression by Herpes Simplex Virus Type 1 or Bovine Herpesvirus 1 Productive Infection.Viruses · 2021Article
- Corrigendum: Intrauterine Viral Infections: Impact of Inflammation on Fetal Neurodevelopment.Frontiers in neuroscience · 2021Article
- Intrauterine Viral Infections: Impact of Inflammation on Fetal Neurodevelopment.Frontiers in neuroscience · 2021Review
- UBE1a Suppresses Herpes Simplex Virus-1 Replication.Viruses · 2020Article
- The ERK-1 function is required for HSV-1-mediated G1/S progression in HEP-2 cells and contributes to virus growth.Scientific reports · 2017Article
- Association of coral algal symbionts with a diverse viral community responsive to heat shock.BMC microbiology · 2017Article
- Intrinsic and Innate Defenses of Neurons: Détente with the Herpesviruses.Journal of virology · 2017Review
- Cullin E3 ligases and their rewiring by viral factors.Biomolecules · 2014Review
- Structural model of ubiquitin transfer onto an artificial RING finger as an E3 ligase.Scientific reports · 2014Article
- Pyrrolidine dithiocarbamate inhibits herpes simplex virus 1 and 2 replication, and its activity may be mediated through dysregulation of the ubiquitin-proteasome system.Journal of virology · 2013Article
- Update on emerging antivirals for the management of herpes simplex virus infections: a patenting perspective.Recent patents on anti-infective drug discovery · 2013Review
- DNA sensing-independent inhibition of herpes simplex virus 1 replication by DAI/ZBP1.Journal of virology · 2013Article
- Kinesin-3 mediates axonal sorting and directional transport of alphaherpesvirus particles in neurons.Cell host & microbe · 2012Article
- Functional characterization of residues required for the herpes simplex virus 1 E3 ubiquitin ligase ICP0 to interact with the cellular E2 ubiquitin-conjugating enzyme UBE2D1 (UbcH5a).Journal of virology · 2012Article
- The molecular basis of herpes simplex virus latency.FEMS microbiology reviews · 2012Review
- The potential link between PML NBs and ICP0 in regulating lytic and latent infection of HSV-1.Protein & cell · 2012Review
- Herpes simplex virus 1 ICP0 phosphorylation site mutants are attenuated for viral replication and impaired for explant-induced reactivation.Journal of virology · 2011Article
- The innate antiviral immune system of the cat: molecular tools for the measurement of its state of activation.Veterinary immunology and immunopathology · 2011Article
- Cytoplasmic localized infected cell protein 0 (bICP0) encoded by bovine herpesvirus 1 inhibits β interferon promoter activity and reduces IRF3 (interferon response factor 3) protein levels.Virus research · 2011Article
13 more citing papers are in PubMed but not listed here.
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4 authors at 1 institution in 1 country.
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Abstract
The infected cell protein 0 (ICP0) of herpes simplex virus 1, a promiscuous transactivator shown to enhance the expression of genes introduced into cells by infection or transfection, interacts with numerous cellular proteins and has been linked to the disruption of ND10 and degradation of several proteins. ICP0 contains a RING finger domain characteristic of a class of E3 ubiquitin ligases. We report that: (i) in infected cells, ICP0 interacts dynamically with proteasomes and is bound to proteasomes in the presence of the proteasome inhibitor MG132. Also in infected cells, cdc34, a polyubiquitinated E2 ubiquitin-conjugating enzyme, exhibits increased ICP0-dependent dynamic interaction with proteasomes. (ii) In an in vitro substrate-independent ubiquitination system, the RING finger domain encoded by exon 2 of ICP0 binds cdc34, whereas the carboxyl-terminal domain of ICP0 functions as an E3 ligase independent of the RING finger domain. The results indicate that ICP0 can act as a unimolecular E3 ubiquitin ligase and that it promotes ubiquitin-protein ligation and binds the E2 cdc34. It differs from other unimolecular E3 ligases in that the domain containing the RING finger binds E2, whereas the ligase activity maps to a different domain of the protein. The results also suggest that ICP0 shuttles between nucleus and cytoplasm as a function of its dynamic interactions with proteasomes.
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