ArticleThe Journal of cell biology1998
Determination of the functional domain organization of the importin alpha nuclear import factor.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 130 citations in OpenAlex.
- Foot-and-mouth disease virus VP4 interferes with host interferon response by targeting the nuclear translocation of interferon regulatory factor 3 (IRF3).Veterinary research · 2026Article
- The functions of herpesvirus shuttling proteins in the virus lifecycle.Frontiers in microbiology · 2025Review
- Identification of the Karyopherin Superfamily in Maize and Its Functional Cues in Plant Development.International journal of molecular sciences · 2022Review
- Regulating Phase Transition in Neurodegenerative Diseases by Nuclear Import Receptors.Biology · 2022Review
- KPNA6 is a Cofactor of ANP32A/B in Supporting Influenza Virus Polymerase Activity.Microbiology spectrum · 2022Article
- Systematic Characterization of the Clinical Relevance of KPNA4 in Pancreatic Ductal Adenocarcinoma.Frontiers in oncology · 2022Article
- Karyopherin abnormalities in neurodegenerative proteinopathies.Brain : a journal of neurology · 2021Review
- Review
- Importin-αs are required for the nuclear localization and function of the Plasmopara viticola effector PvAVH53.Horticulture research · 2021Article
- Importin α: functions as a nuclear transport factor and beyond.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2018Review
- Retinoblastoma-binding Protein 4-regulated Classical Nuclear Transport Is Involved in Cellular Senescence.The Journal of biological chemistry · 2015Article
- Article
- HIV-1 accessory proteins: VpR.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Dynamic trafficking of STAT5 depends on an unconventional nuclear localization signal.Journal of cell science · 2013Article
- Quantitative proteomics reveals regulation of karyopherin subunit alpha-2 (KPNA2) and its potential novel cargo proteins in nonsmall cell lung cancer.Molecular & cellular proteomics : MCP · 2012Article
- Nuclear retention of importin α coordinates cell fate through changes in gene expression.The EMBO journal · 2012Article
- Ran-dependent nuclear export mediators: a structural perspective.The EMBO journal · 2011Review
- Vpr-host interactions during HIV-1 viral life cycle.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2011Review
- HIV-1 accessory protein Vpr: relevance in the pathogenesis of HIV and potential for therapeutic intervention.Retrovirology · 2011Review
- Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr.PloS one · 2011Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although importin alpha (Imp alpha) has been shown to act as the receptor for basic nuclear localization signals (NLSs) and to mediate their recruitment to the importin beta nuclear import factor, little is known about the functional domains present in Imp alpha, with the exception that importin beta binding is known to map close to the Imp alpha NH2 terminus. Here, we demonstrate that sequences essential for binding to the CAS nuclear export factor are located near the Imp alpha COOH terminus and include a critical acidic motif. Although point mutations introduced into this acidic motif inactivated both CAS binding and Imp alpha nuclear export, a putative leucine-rich nuclear export signal proved to be neither necessary nor sufficient for Imp alpha nuclear export. Analysis of sequences within Imp alpha that bind to the SV-40 T antigen NLS or to the similar LEF-1 NLS revealed that both NLSs interact with a subset of the eight degenerate armadillo (Arm) repeats that form the central part of Imp alpha. However, these two NLS-binding sites showed only minimal overlap, thus suggesting that the degeneracy of the Arm repeat region of Imp alpha may serve to facilitate binding to similar but nonidentical basic NLSs. Importantly, the SV-40 T NLS proved able to specifically inhibit the interaction of Imp alpha with CAS in vitro, thus explaining why the SV-40 T NLS is unable to also function as a nuclear export signal.
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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.