ArticleJournal of virology2002
Signals that dictate nuclear, nucleolar, and cytoplasmic shuttling of the gamma(1)34.5 protein of herpes simplex virus type 1.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
44 citing papers in PubMed, 69 citations in OpenAlex.
- HSV ICP27 hijacks host splicing factor SRSF3 to regulate pre-mRNA splicing and export for viral gene expression and immune evasion.PLoS pathogens · 2026Article
- Nucleolar proteins nucleolin and nucleophosmin 1 differentially relocalize during equid alphaherpesvirus 1 (EHV1) infection.Veterinary research communications · 2026Article
- The functions of herpesvirus shuttling proteins in the virus lifecycle.Frontiers in microbiology · 2025Review
- RETRACTED: Regions of Bovine Adenovirus-3 Protein VII Involved in Interactions with Viral and Cellular Proteins.Viruses · 2024Article
- Viral Subversion of the Chromosome Region Maintenance 1 Export Pathway and Its Consequences for the Cell Host.Viruses · 2023Review
- Interplay between Autophagy and Herpes Simplex Virus Type 1: ICP34.5, One of the Main Actors.International journal of molecular sciences · 2022Review
- Herpesvirus-mediated stabilization of ICP0 expression neutralizes restriction by TRIM23.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The herpesvirus accessory protein γ134.5 facilitates viral replication by disabling mitochondrial translocation of RIG-I.PLoS pathogens · 2021Article
- Nuclear and Nucleolar Localization of Bovine Adenovirus-3 Protein V.Frontiers in microbiology · 2020Article
- Comprehensive analysis of nuclear export of herpes simplex virus type 1 tegument proteins and their Epstein-Barr virus orthologs.Traffic (Copenhagen, Denmark) · 2019Article
- Selective Editing of Herpes Simplex Virus 1 Enables Interferon Induction and Viral Replication That Destroy Malignant Cells.Journal of virology · 2019Article
- Herpes Simplex Virus 1 γJournal of virology · 2018Article
- Review
- Herpes Simplex Virus 1 Induces Phosphorylation and Reorganization of Lamin A/C through the γ134.5 Protein That Facilitates Nuclear Egress.Journal of virology · 2016Article
- p32 is a novel target for viral protein ICP34.5 of herpes simplex virus type 1 and facilitates viral nuclear egress.The Journal of biological chemistry · 2014Article
- Article
- Role of immediate early protein ICP27 in the differential sensitivity of herpes simplex viruses 1 and 2 to leptomycin B.Journal of virology · 2013Article
- Herpes simplex virus 2 expresses a novel form of ICP34.5, a major viral neurovirulence factor, through regulated alternative splicing.Journal of virology · 2013Article
- The first identified nucleocytoplasmic shuttling herpesviral capsid protein: herpes simplex virus type 1 VP19C.PloS one · 2012Article
- NoD: a Nucleolar localization sequence detector for eukaryotic and viral proteins.BMC bioinformatics · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The gamma(1)34.5 protein of herpes simplex virus type 1 (HSV-1) is required for viral neurovirulence in vivo. In infected cells, this viral protein prevents the shutoff of protein synthesis mediated by double-stranded-RNA-dependent protein kinase PKR. This is accomplished by recruiting protein phosphatase 1 to dephosphorylate the alpha subunit of translation initiation factor eIF-2 (eIF-2 alpha). Moreover, the gamma(1)34.5 protein is implicated in viral egress and interacts with proliferating cell nuclear antigen. In this report, we show that the gamma(1)34.5 protein encoded by HSV-1(F) is distributed in the nucleus, nucleolus, and cytoplasm in transfected or superinfected cells. Deletion analysis revealed that the Arg-rich cluster from amino acids 1 to 16 in the gamma(1)34.5 protein functions as a nucleolar localization signal. The region from amino acids 208 to 236, containing a bipartite basic amino acid cluster, is able to mediate nuclear localization. R(215)A and R(216)A substitutions in the bipartite motif disrupt this activity. Intriguingly, leptomycin B, an inhibitor of nuclear export, blocks the cytoplasmic accumulation of the gamma(1)34.5 protein. L(134)A and L(136)A substitutions in the leucine-rich motif completely excluded the gamma(1)34.5 protein from the cytoplasm. These results suggest that the gamma(1)34.5 protein continuously shuttles between the nucleus, nucleolus, and cytoplasm, which may be a requirement for the different activities of the gamma(1)34.5 protein in virus-infected cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.