ArticleThe Journal of biological chemistry2013
Interaction of transportin-SR2 with Ras-related nuclear protein (Ran) GTPase.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 13 citations in OpenAlex.
- Abietic acid targets RAN to restrict coxsackievirus B3 infection.Frontiers in microbiology · 2026Article
- Spindle morphology changes between meiosis and mitosis driven by CK2 regulation of the Ran pathway.The Journal of cell biology · 2025Article
- LGMD D2 TNPO3-Related: From Clinical Spectrum to Pathogenetic Mechanism.Frontiers in neurology · 2022Review
- CRISPR/Cas9-Induced Mutagenesis Corroborates the Role of Transportin-SR2 in HIV-1 Nuclear Import.Microbiology spectrum · 2021Article
- Role of Transportin-SR2 in HIV-1 Nuclear Import.Viruses · 2021Review
- HIV-1 Hijacking of Host ATPases and GTPases That Control Protein Trafficking.Frontiers in cell and developmental biology · 2021Review
- Changes in Proteome of Fibroblasts Isolated from Psoriatic Skin Lesions.International journal of molecular sciences · 2020Article
- Inhibitors of the integrase-transportin-SR2 interaction block HIV nuclear import.Retrovirology · 2018Article
- N-terminal half of transportin SR2 interacts with HIV integrase.The Journal of biological chemistry · 2017Article
- The HIV-1 integrase mutant R263A/K264A is 2-fold defective for TRN-SR2 binding and viral nuclear import.The Journal of biological chemistry · 2014Article
- Structure of transportin SR2, a karyopherin involved in human disease, in complex with Ran.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Viral and cellular requirements for the nuclear entry of retroviral preintegration nucleoprotein complexes.Viruses · 2013Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The human immunodeficiency virus type 1 (HIV-1) and other lentiviruses are capable of infecting non-dividing cells and, therefore, need to be imported into the nucleus before integration into the host cell chromatin. Transportin-SR2 (TRN-SR2, Transportin-3, TNPO3) is a cellular karyopherin implicated in nuclear import of HIV-1. A model in which TRN-SR2 imports the viral preintegration complex into the nucleus is supported by direct interaction between TRN-SR2 and HIV-1 integrase (IN). Residues in the C-terminal domain of HIV-1 IN that mediate binding to TRN-SR2 were recently delineated. As for most nuclear import cargoes, the driving force behind HIV-1 preintegration complex import is likely a gradient of the GDP- and GTP-bound forms of Ran, a small GTPase. In this study we offer biochemical and structural characterization of the interaction between TRN-SR2 and Ran. By size exclusion chromatography we demonstrate stable complex formation of TRN-SR2 and RanGTP in solution. Consistent with the behavior of normal nuclear import cargoes, HIV-1 IN is released from the complex with TRN-SR2 by RanGTP. Although in concentrated solutions TRN-SR2 by itself was predominantly present as a dimer, the TRN-SR2-RanGTP complex was significantly more compact. Further analysis supported a model wherein one monomer of TRN-SR2 is bound to one monomer of RanGTP. Finally, we present a homology model of the TRN-SR2-RanGTP complex that is in excellent agreement with the experimental small angle x-ray scattering data.
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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.