ArticleProceedings of the National Academy of Sciences of the United States of America2008
Mutually exclusive interactions drive handover of mRNA from export adaptors to TAP.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 120 papers.
What it found
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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.
The trial behind it
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Who cites it
120 citing papers in PubMed, 197 citations in OpenAlex.
- Temporal gating dictates stress-induced transcript export from the nucleus.Genes & development · 2026Article
- Novel nuclear RNA export factor 1 adaptor drives tumor growth by increasing proliferation-stimulatory mRNA export.Signal transduction and targeted therapy · 2026Article
- Temporal gating dictates stress-induced transcript export from the nucleus.bioRxiv : the preprint server for biology · 2026Article
- Molecular insights into mRNA export regulation by the human TREX-2 complex.Nature communications · 2026Article
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026Review
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- Two RNA-Binding Regions of PCID2, a Subunit of the TREX-2 mRNA Nuclear Export Complex, Competitively Interact with the 3' Noncoding Region of ras2 mRNA.Doklady. Biochemistry and biophysics · 2025Article
- Interdomain Interactions of the PCID2 Protein, One of the Subunits of the TREX-2 mRNA Export Complex in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2025Article
- Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025Article
- Decoding protein-RNA interactions using CLIP-based methodologies.Nature reviews. Genetics · 2024Review
- An integrated analysis of multiple datasets reveals novel gene signatures in human granulosa cells.Scientific data · 2024Article
- Nuclear mRNA export.Acta biochimica et biophysica Sinica · 2024Review
- Review
- TREX tetramer disruption alters RNA processing necessary for corticogenesis in THOC6 Intellectual Disability Syndrome.Nature communications · 2024Article
- mRNA nuclear export: how mRNA identity features distinguish functional RNAs from junk transcripts.RNA biology · 2024Review
- Viral Subversion of the Chromosome Region Maintenance 1 Export Pathway and Its Consequences for the Cell Host.Viruses · 2023Review
- The master energy homeostasis regulator PGC-1α exhibits an mRNA nuclear export function.Nature communications · 2023Article
- Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023Review
60 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Adaptor proteins stimulate the nuclear export of mRNA, but their mechanism of action remains unclear. Here, we show that REF/ALY binds mRNA; but upon formation of a ternary complex with TAP the RNA is transferred from REF to TAP, and overexpression of TAP displaces REF from mRNA in vivo. RNA is also handed over from two other adaptors, 9G8 and SRp20 to TAP upon formation of a ternary complex. Interestingly, the RNA-binding affinity of TAP is enhanced 4-fold in vitro once it is complexed with REF. 9G8 and SRp20 also enhance the TAP RNA-binding activity in vitro. Consistent with a model in which TAP directly binds mRNA handed over from adaptors during export, we show that TAP binds mRNA in vivo by an arginine-rich motif in its N-terminal domain. The importance of direct TAP-mRNA interactions is confirmed by the observation that a mutant form of TAP that fails to bind mRNA but retains the ability to bind REF does not function in mRNA export.
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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.