ArticleMolecular and cellular biology2002
Nuclear export of mRNA by TAP/NXF1 requires two nucleoporin-binding sites but not p15.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 100 citations in OpenAlex.
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- O-GlcNAc modulation of nuclear pore complexes orchestrates mRNA export efficiency.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Sending the message: specialized RNA export mechanisms in trypanosomes.Trends in parasitology · 2022Review
- Distinct roles of nuclear basket proteins in directing the passage of mRNA through the nuclear pore.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Selective nuclear export of mRNAs is promoted by DRBD18 in Trypanosoma brucei.Molecular microbiology · 2021Article
- Review
- The RNA-Binding Protein SBR (Dm NXF1) Is Required for the Constitution of Medulla Boundaries inCells · 2021Article
- Nucleocytoplasmic Transport: Regulatory Mechanisms and the Implications in Neurodegeneration.International journal of molecular sciences · 2021Review
- A novel assay provides insight into tRNAPhe retrograde nuclear import and re-export in S. cerevisiae.Nucleic acids research · 2020Article
- Molecular mechanism underlying selective inhibition of mRNA nuclear export by herpesvirus protein ORF10.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- A Pandas complex adapted for piRNA-guided transcriptional silencing and heterochromatin formation.Nature cell biology · 2019Article
- The general mRNA exporters Mex67 and Mtr2 play distinct roles in nuclear export of tRNAs in Trypanosoma brucei.Nucleic acids research · 2019Article
- Article
- The nascent RNA binding complex SFiNX licenses piRNA-guided heterochromatin formation.Nature structural & molecular biology · 2019Article
- The coming-of-age of nucleocytoplasmic transport in motor neuron disease and neurodegeneration.Cellular and molecular life sciences : CMLS · 2019Review
- Nuclear export of mRNA molecules studied by SPEED microscopy.Methods (San Diego, Calif.) · 2019Review
- Mediated nuclear import and export of TAZ and the underlying molecular requirements.Nature communications · 2018Article
- Epstein-Barr Virus-Induced Nodules on Viral Replication Compartments Contain RNA Processing Proteins and a Viral Long Noncoding RNA.Journal of virology · 2018Article
- Sharing the load: Mex67-Mtr2 cofunctions with Los1 in primary tRNA nuclear export.Genes & development · 2017Article
- A short conserved motif in ALYREF directs cap- and EJC-dependent assembly of export complexes on spliced mRNAs.Nucleic acids research · 2016Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metazoan NXF1/p15 heterodimers promote export of bulk mRNA through nuclear pore complexes (NPC). NXF1 interacts with the NPC via two distinct structural domains, the UBA-like domain and the NTF2-like scaffold, which results from the heterodimerization of the NTF2-like domain of NXF1 with p15. Both domains feature a single nucleoporin-binding site, and they act synergistically to promote NPC translocation. Whether the NTF2-like scaffold (and thereby p15) contributes only to NXF1/NPC association or is also required for other functions, e.g., to impart directionality to the export process by regulating NXF1/NPC or NXF1/cargo interactions, remains unresolved. Here we show that a minimum of two nucleoporin-binding sites is required for NXF1-mediated export of cellular mRNA. These binding sites can be provided by an NTF2-like scaffold followed by a UBA-like domain (as in the wild-type protein) or by two NTF2-like scaffolds or two UBA-like domains in tandem. In the latter case, the export activity of NXF1 is independent of p15. Thus, as for the UBA-like domain, the function of the NTF2-like scaffold is confined to nucleoporin binding. More importantly, two copies of either of these domains are sufficient to promote directional transport of mRNA cargoes across the NPC.
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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.