ArticleMolecular & cellular proteomics : MCP2014
Identification of importin α 7 specific transport cargoes using a proteomic screening approach.
Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 22 citations in OpenAlex.
- Zika virus recruits karyopherin α6 for efficient replication via NS2B.Journal of virology · 2026Article
- TMCO1 is upregulated in breast cancer and regulates the response to pro-apoptotic agents in breast cancer cells.Cell death discovery · 2024Article
- Characterization of the nuclear import of the human CHD4-NuRD complex.Journal of cell science · 2023Article
- Proteomic elucidation of the targets and primary functions of the picornavirus 2A protease.The Journal of biological chemistry · 2022Article
- Non-transport roles of nuclear import receptors: In need of the right balance.Frontiers in cell and developmental biology · 2022Review
- The Molecular Function of PURA and Its Implications in Neurological Diseases.Frontiers in genetics · 2021Review
- HECTD1 regulates the expression of SNAIL: Implications for epithelial‑mesenchymal transition.International journal of oncology · 2020Article
- Importin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.PLoS pathogens · 2018Article
- Targeting Importin-α7 as a Therapeutic Approach against Pandemic Influenza Viruses.Journal of virology · 2015Article
- Diversification of importin-α isoforms in cellular trafficking and disease states.The Biochemical journal · 2015Review
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The importin α:β complex is responsible for the nuclear import of proteins bearing classical nuclear localization signals. In mammals, several importin α subtypes are known to exist that are suggested to have individual functions. Importin α 7 was shown to play a crucial role in early embryonic development in mice. Embryos from importin α 7-depleted females stop at the two-cell stage and show disturbed zygotic genome activation. As there is evidence that individual importin α subtypes possess cargo specificities, we hypothesized that importin α 7 binds a unique set of intracellular proteins. With the use of a collection of in vitro and in vivo binding assays, importin α 7 interaction partners were identified that differed from proteins found to bind to importin α 2 and 3. One of the proteins preferentially binding importin α 7 was the maternal effect protein Brg1. However, Brg1 was localized in oocyte nuclei in importin α 7-deficient embryos, albeit in reduced amounts, suggesting additional modes of nuclear translocation of this factor. An additional SILAC-based screening approach identified Ash2l, Chd3, Mcm3, and Smarcc1, whose nuclear import seems to be disturbed in importin α 7-deficient fibroblasts.
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