ArticleThe Journal of cell biology2002
Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
87 citing papers in PubMed, 181 citations in OpenAlex.
- Mechanisms of microRNA trafficking to mitochondria in the heart.Current opinion in physiology · 2025Article
- RNA Through Time: From the Origin of Life to Therapeutic Frontiers in Transcriptomics and Epitranscriptional Medicine.International journal of molecular sciences · 2025Review
- Phosphate-dependent nuclear export via a non-classical NES class recognized by exportin Msn5.Nature communications · 2025Article
- Circular RNA circPHLPP2 promotes tumor growth and anti-PD-1 resistance through binding ILF3 to regulate IL36γ transcription in colorectal cancer.Molecular cancer · 2024Article
- Exploring Cellular Gateways: Unraveling the Secrets of Disordered Proteins within Live Nuclear Pores.Research square · 2024Article
- The competitive landscape of the dsRNA world.Molecular cell · 2024Review
- Lipid kinase PIP5K1A regulates let-7 microRNA biogenesis through interacting with nuclear export protein XPO5.Nucleic acids research · 2023Article
- Article
- Regulated dicing of pre-mir-144 via reshaping of its terminal loop.Nucleic acids research · 2022Article
- Article
- Selectivity of Exportin 5 binding to human precursor microRNAs.RNA biology · 2021Article
- Article
- MicroRNA-375 overexpression disrupts cardiac development of Zebrafish (Danio rerio) by targeting notch2.Protoplasma · 2020Article
- Trafficking of siRNA precursors by the dsRBD protein Blanks in Drosophila.Nucleic acids research · 2020Article
- XPO5 promotes primary miRNA processing independently of RanGTP.Nature communications · 2020Article
- Single-Nucleotide Polymorphisms inBiochemistry research international · 2020Article
- The general mRNA exporters Mex67 and Mtr2 play distinct roles in nuclear export of tRNAs in Trypanosoma brucei.Nucleic acids research · 2019Article
- RNA regulatory processes in RNA virus biology.Wiley interdisciplinary reviews. RNA · 2019Review
- An ARF6-Exportin-5 axis delivers pre-miRNA cargo to tumour microvesicles.Nature cell biology · 2019Article
- The coming-of-age of nucleocytoplasmic transport in motor neuron disease and neurodegeneration.Cellular and molecular life sciences : CMLS · 2019Review
27 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
We have identified a novel human karyopherin (Kap) beta family member that is related to human Crm1 and the Saccharomyces cerevisiae protein, Msn5p/Kap142p. Like other known transport receptors, this Kap binds specifically to RanGTP, interacts with nucleoporins, and shuttles between the nuclear and cytoplasmic compartments. We report that interleukin enhancer binding factor (ILF)3, a double-stranded RNA binding protein, associates with this Kap in a RanGTP-dependent manner and that its double-stranded RNA binding domain (dsRBD) is the limiting sequence required for this interaction. Importantly, the Kap interacts with dsRBDs found in several other proteins and binding is blocked by double-stranded RNA. We find that the dsRBD of ILF3 functions as a novel nuclear export sequence (NES) in intact cells, and its ability to serve as an NES is dependent on the expression of the Kap. In digitonin-permeabilized cells, the Kap but not Crm1 stimulated nuclear export of ILF3. Based on the ability of this Kap to mediate the export of dsRNA binding proteins, we named the protein exportin-5. We propose that exportin-5 is not an RNA export factor but instead participates in the regulated translocation of dsRBD proteins to the cytoplasm where they interact with target mRNAs.
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Registered trials
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.