ArticleMolecular and cellular biology1999
Importin beta can mediate the nuclear import of an arginine-rich nuclear localization signal in the absence of importin alpha.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.
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Who cites it
89 citing papers in PubMed, 214 citations in OpenAlex.
- Overcoming the nuclear barrier in nonviral gene therapy: mechanisms, carrier design, and translational perspectives on NLS peptide and DNA targeting sequence strategies.Drug delivery · 2026Review
- Nucleomodulins from gut bacteria: diverse mechanisms of translocation and interaction with host nuclear processes.Applied and environmental microbiology · 2025Review
- Retroviral adapters hijack the RNA helicase UPF1 in a CRM1/XPO1-dependent manner and reveal proviral roles of UPF1.Nucleic acids research · 2025Article
- Nuclear localization signal-tagged systems: relevant nuclear import principles in the context of current therapeutic design.Chemical Society reviews · 2024Review
- The nuclear entry of the aryl hydrocarbon receptor (AHR) relies on the first nuclear localization signal and can be negatively regulated through IMPα/β specific inhibitors.Scientific reports · 2023Article
- Application of Super-resolution SPEED Microscopy in the Study of Cellular Dynamics.Chemical & biomedical imaging · 2023Review
- Nucleocytoplasmic Shuttling of Porcine Parvovirus NS1 Protein Mediated by the CRM1 Nuclear Export Pathway and the Importin α/β Nuclear Import Pathway.Journal of virology · 2022Article
- Inhibition of Kpnβ1 mediated nuclear import enhances cisplatin chemosensitivity in cervical cancer.BMC cancer · 2021Article
- Analysis of insect nuclear small heat shock proteins and interacting proteins.Cell stress & chaperones · 2021Article
- Trnp1 organizes diverse nuclear membrane-less compartments in neural stem cells.The EMBO journal · 2020Article
- Cytoplasmic Parvovirus Capsids Recruit Importin Beta for Nuclear Delivery.Journal of virology · 2020Article
- Characterization of Nucleocytoplasmic Shuttling of Pseudorabies Virus Protein UL46.Frontiers in veterinary science · 2020Article
- A universal transportin protein drives stochastic choice of olfactory neurons via specific nuclear import of aProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Heterogeneous Nuclear Ribonucleoprotein A1 and Lamin A/C Modulate Nucleocytoplasmic Shuttling of Avian Reovirus p17.Journal of virology · 2019Article
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- Nuclear Import of Hepatitis B Virus Capsids and Genome.Viruses · 2017Review
- Is unphosphorylated Rex, as multifunctional protein of HTLV-1, a fully intrinsically disordered protein? An in silico study.Biochemistry and biophysics reports · 2016Article
- RNA-binding protein HuR regulates nuclear import of protein.Journal of cell science · 2016Article
29 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The import of proteins into the nucleus is dependent on cis-acting targeting sequences, nuclear localization signals (NLSs), and members of the nuclear transport receptor (importin-beta-like) superfamily. The most extensively characterized import pathway, often termed the classical pathway, is utilized by many basic-type (lysine-rich) NLSs and requires an additional component, importin alpha, to serve as a bridge between the NLS and the import receptor importin beta. More recently, it has become clear that a variety of proteins enter the nucleus via alternative import receptors and that their NLSs bind directly to those receptors. By using the digitonin-permeabilized cell system for protein import in vitro, we have defined the import pathway for the Rex protein of human T-cell leukemia virus type 1. Interestingly, the arginine-rich NLS of Rex uses importin beta for import but does so by a mechanism that is importin alpha independent. Based on the ability of the Rex NLS to inhibit the import of the lysine-rich NLS of T antigen and of both NLSs to be inhibited by the domain of importin alpha that binds importin beta (the IBB domain), we infer that the Rex NLS interacts with importin beta directly. In addition, and in keeping with other receptor-mediated nuclear import pathways, Rex import is dependent on the integrity of the Ran GTPase cycle. Based on these results, we suggest that importin beta can mediate the nuclear import of arginine-rich NLSs directly, or lysine-rich NLSs through the action of importin alpha.
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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.