ArticleJournal of virology2010
Pseudorabies virus tegument protein Us2 recruits the mitogen-activated protein kinase extracellular-regulated kinase (ERK) to membranes through interaction with the ERK common docking domain.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Duck plague virus US2 promotes p62-mediated autophagic degradation of RIG-I to suppress antiviral signaling.Poultry science · 2026Article
- The prenylated pUS2 protein of pseudorabies virus contributes to phosphorylation of connexin 43 and suppression of gap junctional intercellular communication.Journal of virology · 2026Article
- Duck plague virus LORF2 utilizes RNF34 to inhibit antiviral innate immunity by ubiquitination and degradation of IRF7.PLoS pathogens · 2026Article
- Pseudorabies virus tegument protein US2 antagonizes antiviral innate immunity by targeting cGAS-STING signaling pathway.Frontiers in immunology · 2024Article
- The Attenuated Pseudorabies Virus Vaccine Strain Bartha Hyperactivates Plasmacytoid Dendritic Cells by Generating Large Amounts of Cell-Free Virus in Infected Epithelial Cells.Journal of virology · 2022Article
- The Attenuated Pseudorabies Virus Vaccine Strain Bartha K61: A Brief Review on the Knowledge Gathered During 60 Years of Research.Pathogens (Basel, Switzerland) · 2020Review
- Newcastle Disease Virus V Protein Promotes Viral Replication in HeLa Cells through the Activation of MEK/ERK Signaling.Viruses · 2018Article
- Deletion of pseudorabies virus US2 gene enhances viral titers in a porcine cerebral cortex primary culture system.Virus genes · 2018Article
- Comparison of Pathogenicity-Related Genes in the Current Pseudorabies Virus Outbreak in China.Scientific reports · 2017Article
- The Pseudorabies Virus Glycoprotein gE/gI Complex Suppresses Type I Interferon Production by Plasmacytoid Dendritic Cells.Journal of virology · 2017Article
- Pseudorabies virus triggers glycoprotein gE-mediated ERK1/2 activation and ERK1/2-dependent migratory behavior in T cells.Journal of virology · 2015Article
- Pseudorabies virus pUL46 induces activation of ERK1/2 and regulates herpesvirus-induced nuclear envelope breakdown.Journal of virology · 2014Article
- The Us2 gene product of herpes simplex virus 2 is a membrane-associated ubiquitin-interacting protein.Journal of virology · 2013Article
- Suppression of extracellular signal-regulated kinase activity in herpes simplex virus 1-infected cells by the Us3 protein kinase.Journal of virology · 2012Article
- Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdown.Journal of virology · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The pseudorabies virus (PRV) Us2 protein binds to the extracellular-regulated kinase (ERK) and inhibits the activation of ERK nuclear targets by sequestering cytoplasmic ERK on cellular membranes. Utilizing a series of Us2 truncations, we determined that the minimal portion of Us2 required for interaction with ERK is contained within its amino-terminal 214 amino acids. The loss of the ability of Us2 to bind to ERK in coimmunoprecipitation experiments was accompanied by a failure of Us2 to form oligomers, raising the possibility that higher-order Us2 structures are required for ERK interaction. To map the Us2 interaction site on ERK, we introduced mutations into the region of ERK that interacts with the ERK kinase, MEK, or into the common docking (CD) domain that mediates interactions with many ERK substrates. ERK carrying mutations within the MEK binding region maintained the ability to bind Us2, whereas ERK carrying mutations within the CD domain did not. Furthermore, the ERK CD domain was required for the Us2-mediated recruitment of ERK to membranes. Taken together, these findings suggest that Us2 regulates ERK activity by spatially restricting ERK localization and also by interfering with select ERK-substrate interactions.
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Registered trials
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.