ArticleMolecular biology of the cell2005
The functionally conserved nucleoporins Nup124p from fission yeast and the human Nup153 mediate nuclear import and activity of the Tf1 retrotransposon and HIV-1 Vpr.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it, 42 citations in OpenAlex.
- Host cell factors in HIV replication: meta-analysis of genome-wide studies.PLoS pathogens · 2009Pooled it
- Crosstalk between nucleocytoplasmic trafficking and the innate immune response to viral infection.The Journal of biological chemistry · 2021Review
- Contribution of yeast models to virus research.Applied microbiology and biotechnology · 2021Review
- Viral protein X unlocks the nuclear pore complex through a human Nup153-dependent pathway to promote nuclear translocation of the lentiviral genome.Molecular biology of the cell · 2020Article
- Extra-Low-Frequency Pulse Stimulated Conformational Change in Blood-Cell Proteins and Consequent Immune Activity Transformation.IEEE journal of translational engineering in health and medicine · 2020Article
- Review
- Nup2 performs diverse interphase functions in Aspergillus nidulans.Molecular biology of the cell · 2018Article
- The yeast Ty1 retrotransposon requires components of the nuclear pore complex for transcription and genomic integration.Nucleic acids research · 2018Article
- Host factors that promote retrotransposon integration are similar in distantly related eukaryotes.PLoS genetics · 2017Article
- Integration site selection by retroviruses and transposable elements in eukaryotes.Nature reviews. Genetics · 2017Review
- The effects of natural selection across molecular pathways in Drosophila melanogaster.BMC evolutionary biology · 2015Article
- The Long Terminal Repeat Retrotransposons Tf1 and Tf2 of Schizosaccharomyces pombe.Microbiology spectrum · 2015Review
- Nup2 requires a highly divergent partner, NupA, to fulfill functions at nuclear pore complexes and the mitotic chromatin region.Molecular biology of the cell · 2015Article
- Profiling of alternative polyadenylation sites in luminal B breast cancer using the SAPAS method.International journal of molecular medicine · 2015Article
- The Nup153-Nup50 protein interface and its role in nuclear import.The Journal of biological chemistry · 2012Article
- Cellular cofactors of lentiviral integrase: from target validation to drug discovery.Molecular biology international · 2012Article
- The HIV-1 passage from cytoplasm to nucleus: the process involving a complex exchange between the components of HIV-1 and cellular machinery to access nucleus and successful integration.International journal of biochemistry and molecular biology · 2012Article
- The requirement for nucleoporin NUP153 during human immunodeficiency virus type 1 infection is determined by the viral capsid.Journal of virology · 2011Article
- Vpr-host interactions during HIV-1 viral life cycle.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2011Review
- LEDGF dominant interference proteins demonstrate prenuclear exposure of HIV-1 integrase and synergize with LEDGF depletion to destroy viral infectivity.Journal of virology · 2011Article
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report that the fission yeast nucleoporin Nup124p is required for the nuclear import of both, retrotransposon Tf1-Gag as well as the retroviral HIV-1 Vpr. Failure to import Tf1-Gag into the nucleus in a nup124 null mutant resulted in complete loss of Tf1 transposition. Similarly, nuclear import of HIV-1 Vpr was impaired in nup124 null mutant strains and cells became resistant to Vpr's cell-killing activity. On the basis of protein domain similarity, the human nucleoporin Nup153 was identified as a putative homolog of Nup124p. We demonstrate that in vitro-translated Nup124p and Nup153 coimmunoprecipitate Tf1-Gag or HIV-1 Vpr. Though full-length Nup153 was unable to complement the Tf1 transposition defect in a nup124 null mutant, we provide evidence that both nucleoporins share a unique N-terminal domain, Nup124p(AA264-454) and Nup153(AA448-634) that is absolutely essential for Tf1 transposition. Epigenetic overexpression of this domain in a wild-type (nup124(+)) background blocked Tf1 activity implying that sequences from Nup124p and the human Nup153 challenged the same pathway affecting Tf1 transposition. Our results establish a unique relationship between two analogous nucleoporins Nup124p and Nup153 wherein the function of a common domain in retrotransposition is conserved.
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