ArticleJournal of virology2000
Interaction between herpes simplex virus type 1 IE63 protein and cellular protein p32.
Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 60 citations in OpenAlex.
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- Multi-proteomic profiling of the varicella-zoster virus-host interface reveals host susceptibilities to severe infection.Nature microbiology · 2025Article
- Serine/Threonine Protein Kinases as Attractive Targets for Anti-Cancer Drugs-An Innovative Approach to Ligand Tuning Using Combined Quantum Chemical Calculations, Molecular Docking, Molecular Dynamic Simulations, and Network-like Similarity Graphs.Molecules (Basel, Switzerland) · 2024Article
- Protein Kinase CK2 and Epstein-Barr Virus.Biomedicines · 2023Review
- Leaked Mitochondrial C1QBP Inhibits Activation of the DNA Sensor cGAS.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- Noncytotoxic functions of killer cell granzymes in viral infections.PLoS pathogens · 2021Review
- Article
- Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear Egress.Journal of virology · 2015Article
- Review
- A proteomic approach to discover and compare interacting partners of papillomavirus E2 proteins from diverse phylogenetic groups.Proteomics · 2015Article
- Heterogeneous nuclear ribonucleoprotein K (hnRNP-K) promotes tumor metastasis by induction of genes involved in extracellular matrix, cell movement, and angiogenesis.The Journal of biological chemistry · 2013Article
- Interaction network of proteins associated with human cytomegalovirus IE2-p86 protein during infection: a proteomic analysis.PloS one · 2013Article
- Herpes simplex virus ICP27 protein directly interacts with the nuclear pore complex through Nup62, inhibiting host nucleocytoplasmic transport pathways.The Journal of biological chemistry · 2012Article
- Host factors in enterovirus 71 replication.Journal of virology · 2011Review
- Structure of the Trypanosoma brucei p22 protein, a cytochrome oxidase subunit II-specific RNA-editing accessory factor.The Journal of biological chemistry · 2010Article
- Herpes simplex virus type 1 ICP27 regulates expression of a variant, secreted form of glycoprotein C by an intron retention mechanism.Journal of virology · 2008Article
- Identification of human cytomegalovirus UL84 virus- and cell-encoded binding partners by using proteomics analysis.Journal of virology · 2008Article
- Protein kinase CK2 phosphorylation of EB2 regulates its function in the production of Epstein-Barr virus infectious viral particles.Journal of virology · 2007Article
- Herpes simplex virus type 1 ICP27-dependent activation of NF-kappaB.Journal of virology · 2006Article
- Acetylated Tat regulates human immunodeficiency virus type 1 splicing through its interaction with the splicing regulator p32.Journal of virology · 2006Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The herpes simplex virus type 1 (HSV-1) immediate-early gene IE63 (ICP27), the only HSV-1 regulatory gene with a homologue in every mammalian and avian herpesvirus sequenced so far, is a multifunctional protein which regulates transcriptional and posttranscriptional processes. One of its posttranscriptional effects is the inhibition of splicing of viral and cellular transcripts. We previously identified heterogeneous nuclear ribonucleoprotein (hnRNP) K and casein kinase 2 (CK2) as two protein partners of IE63 (H. Bryant et al., J. Biol. Chem. 274:28991-28998, 1999). Here, using a yeast two-hybrid assay, we identify another partner of IE63, the cellular protein p32. Confirmation of this interaction was provided by coimmunoprecipitation from virus-infected cells and recombinant p32 binding assays. A p32-hnRNP K-CK2 complex, which required IE63 to form, was isolated from HSV-1-infected cells, and coimmunoprecipitating p32 was phosphorylated by CK2. Expression of IE63 altered the cytoplasmic distribution of p32, with some now colocalizing with IE63 in the nuclei of infected and transfected cells. As p32 copurifies with splicing factors and can inhibit splicing, we propose that IE63 together with p32, possibly with other IE63 partner proteins, acts to disrupt or regulate pre-mRNA splicing. As well as contributing to host cell shutoff, this effect could facilitate splicing-independent nuclear export of viral transcripts.
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Registered trials
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