ArticleThe Journal of biological chemistry2013
Several phenylalanine-glycine motives in the nucleoporin Nup214 are essential for binding of the nuclear export receptor CRM1.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 36 citations in OpenAlex.
- Enhanced nuclear export caused by O-GlcNAcylation of nucleoporins is a potential therapeutic target in mesothelioma.British journal of cancer · 2026Article
- Unusual Presentation ofInternational journal of molecular sciences · 2023Article
- SET-CAN/NUP214 fusion gene in leukemia: general features and clinical advances.Frontiers in oncology · 2023Review
- Spelling out the roles of individual nucleoporins in nuclear export of mRNA.Nucleus (Austin, Tex.) · 2022Review
- 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.Protein & cell · 2022Article
- CRM1 Promotes Capsid Disassembly and Nuclear Envelope Translocation of Adenovirus Independently of Its Export Function.Journal of virology · 2022Article
- Nuclear export of the pre-60S ribosomal subunit through single nuclear pores observed in real time.Nature communications · 2021Article
- Measuring and Interpreting Nuclear Transport in Neurodegenerative Disease-The Example of C9orf72 ALS.International journal of molecular sciences · 2021Review
- Nuclear Import Receptors Directly Bind to Arginine-Rich Dipeptide Repeat Proteins and Suppress Their Pathological Interactions.Cell reports · 2020Article
- Nup358 and Transportin 1 Cooperate in Adenoviral Genome Import.Journal of virology · 2020Article
- Article
- NUP214 in Leukemia: It's More than Transport.Cells · 2019Review
- Article
- Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1.Scientific reports · 2018Article
- The Oncogenic Fusion Proteins SET-Nup214 and Sequestosome-1 (SQSTM1)-Nup214 Form Dynamic Nuclear Bodies and Differentially Affect Nuclear Protein and Poly(A)+ RNA Export.The Journal of biological chemistry · 2016Article
- The selective permeability barrier in the nuclear pore complex.Nucleus (Austin, Tex.) · 2016Review
- Leukemia-Associated Nup214 Fusion Proteins Disturb the XPO1-Mediated Nuclear-Cytoplasmic Transport Pathway and Thereby the NF-κB Signaling Pathway.Molecular and cellular biology · 2016Article
- Chromatin-prebound Crm1 recruits Nup98-HoxA9 fusion to induce aberrant expression of Hox cluster genes.eLife · 2016Article
- Review
- Nucleoporin FG domains facilitate mRNP remodeling at the cytoplasmic face of the nuclear pore complex.Genetics · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nucleoporins containing phenylalanine glycine (FG) repeats play an important role in nucleocytoplasmic transport as they bind to transport receptors and mediate translocation of transport complexes across the nuclear pore complex (NPC). Nup214/CAN, a nucleoporin that is found at the cytoplasmic side of the NPC, interacts with both import and export receptors. In functional assays, dominant-negative fragments of Nup214 inhibited CRM1-dependent nuclear export, as the export receptor became rate-limiting. Several nuclear import pathways, by contrast, were not affected by the Nup214 fragments. We now characterize the CRM1-binding region of Nup214 in detail and identify several FG motives that are required for this interaction. Our results support a model where CRM1, like other transport receptors, contacts FG-Nups via multiple binding sites.
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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.