ArticleMolecular biology of the cell2003
Importin beta-depending nuclear import pathways: role of the adapter proteins in the docking and releasing steps.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 32 citations in OpenAlex.
- From the Cytoplasm into the Nucleus-Hepatitis B Virus Travel and Genome Repair.Microorganisms · 2025Review
- Time-resolved biophysical approaches to nucleocytoplasmic transport.Computational and structural biotechnology journal · 2017Review
- Snail nuclear transport: the gateways regulating epithelial-to-mesenchymal transition?Seminars in cancer biology · 2014Review
- Importin β-dependent nuclear import of TopBP1 in ATR-Chk1 checkpoint in Xenopus egg extracts.Cellular signalling · 2014Article
- Axonal transcription factors: novel regulators of growth cone-to-nucleus signaling.Developmental neurobiology · 2014Review
- The importin β binding domain as a master regulator of nucleocytoplasmic transport.Biochimica et biophysica acta · 2011Review
- The importin beta binding domain modulates the avidity of importin beta for the nuclear pore complex.The Journal of biological chemistry · 2010Article
- A synthetic snRNA m3G-CAP enhances nuclear delivery of exogenous proteins and nucleic acids.Nucleic acids research · 2009Article
- Functional association of Sun1 with nuclear pore complexes.The Journal of cell biology · 2007Article
- Predicting the nuclear localization signals of 107 types of HPV L1 proteins by bioinformatic analysis.Genomics, proteomics & bioinformatics · 2006Article
- In vivo analysis of importin alpha proteins reveals cellular proliferation inhibition and substrate specificity.Molecular and cellular biology · 2004Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nuclear imports of uridine-rich small nuclear ribonucleoprotein (U1 snRNP) and proteins with classical nuclear localization signal (cNLS-protein) are mediated by importin beta. However, due to the presence of different import signals, the adapter protein of the imported molecules and importin beta is different for each pathway. Although the adapter for cNLS-protein is importin alpha, the adapter for U1 snRNP is snurportin1 (SPN1). Herein, we show that the use of distinct adapters by importin beta results in differences at the docking and releasing step for these two import pathways. Nuclear pore complex (NPC) docking of U1 snRNP but not of cNLS-protein was inhibited by an anti-CAN/Nup214 antibody. Thus, the initial NPC-binding site is different for each pathway. Pull-down assays between immobilized SPN1 and two truncated forms of importin beta documented that SPN1 and importin alpha have different binding sites on importin beta. Importin beta fragment 1-618, which binds to SPN1 but not to importin alpha, was able to support the nuclear import of U1 snRNPs. After the translocation through the NPC, both import complexes associated with the nuclear side of the NPC. However, we found that the nature of the importin beta-binding domain of the adapters influences the release of the cargo into the nucleoplasm.
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