ArticleJournal of virology2009
Mengovirus-induced rearrangement of the nuclear pore complex: hijacking cellular phosphorylation machinery.
Article in Journal of virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- Cardiac α2δ1 C-terminal contributes to left atrial hypertrophy in chronic ischemic heart failure, in association with changes in membrane GluN1 and p-CAMKII/p-HDAC4 signaling.Cell and tissue research · 2026Article
- The leader proteins of Theiler's virus and Boone cardiovirus use a combination of short linear motifs (SLiMs) to target RSK kinases to the nuclear pore complex.Journal of virology · 2025Article
- Modulation of Ire1-Xbp1 Defense Pathway in Encephalomyocarditis Virus-Infected HeLa Cells.Viruses · 2025Article
- Comprehensive Elucidation of the Role of L and 2A Security Proteins on Cell Death during EMCV Infection.Viruses · 2024Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- Viral Subversion of the Chromosome Region Maintenance 1 Export Pathway and Its Consequences for the Cell Host.Viruses · 2023Review
- Cardiovirus leader proteins retarget RSK kinases toward alternative substrates to perturb nucleocytoplasmic traffic.PLoS pathogens · 2022Article
- Article
- Insights from structural studies of the cardiovirus 2A protein.Bioscience reports · 2022Review
- Review
- Review
- SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Addressing Non-linear System Dynamics of Single-Strand RNA Virus-Host Interaction.Frontiers in microbiology · 2020Article
- The Strengths of Scanning Electron Microscopy in Deciphering SARS-CoV-2 Infectious Cycle.Frontiers in microbiology · 2020Article
- The Leader Protein of Theiler's Virus Prevents the Activation of PKR.Journal of virology · 2019Article
- Characterization of the stimulators of protein-directed ribosomal frameshifting in Theiler's murine encephalomyelitis virus.Nucleic acids research · 2019Article
- Protein phosphatases at the nuclear envelope.Biochemical Society transactions · 2018Review
- Functional roles of HIV-1 Tat protein in the nucleus.Cellular and molecular life sciences : CMLS · 2016Review
- Selective Removal of FG Repeat Domains from the Nuclear Pore Complex by Enterovirus 2A(pro).Journal of virology · 2015Article
- Three cardiovirus Leader proteins equivalently inhibit four different nucleocytoplasmic trafficking pathways.Virology · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Representatives of several picornavirus genera have been shown previously to significantly enhance non-controllable bidirectional exchange of proteins between nuclei and cytoplasm. In enteroviruses and rhinoviruses, enhanced permeabilization of the nuclear pores appears to be primarily due to proteolytic degradation of some nucleoporins (protein components of the pore), whereas this effect in cardiovirus-infected cells is triggered by the leader (L) protein, devoid of any enzymatic activities. Here, we present evidence that expression of L alone was sufficient to cause permeabilization of the nuclear envelope in HeLa cells. In contrast to poliovirus, mengovirus infection of these cells did not elicit loss of nucleoporins Nup62 and Nup153 from the nuclear pore complex. Instead, nuclear envelope permeabilization was accompanied by hyperphosphorylation of Nup62 in cells infected with wild-type mengovirus, whereas both of these alterations were suppressed in L-deficient virus mutants. Since phosphorylation of Nup62 (although less prominent) did accompany permeabilization of the nuclear envelope prior to its mitotic disassembly in uninfected cells, we hypothesize that cardiovirus L alters the nucleocytoplasmic traffic by hijacking some components of the normal cell division machinery. The variability and biological significance of picornaviral interactions with the nucleocytoplasmic transport in the infected cells are discussed.
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