ArticleMolecular and cellular biology2008
ATP-dependent recruitment of export factor Aly/REF onto intronless mRNAs by RNA helicase UAP56.
Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 116 citations in OpenAlex.
- In Vitro RNA-Protein Binding Assays to Identify RNA Helicases for U snRNA Nuclear Export.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Conserved mRNP remodeling mechanism of the TREX-2.1 complex.Nucleic acids research · 2026Article
- The role of phase separation for RNA and protein transport through the nuclear pore complex.Journal of experimental botany · 2026Review
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- Identification of RNA binding proteins that mediate a quality control mechanism of splicing.bioRxiv : the preprint server for biology · 2025Article
- The RNA helicase DDX39 contributes to the nuclear export of spliceosomal U snRNA by loading of PHAX onto RNA.Nucleic acids research · 2024Article
- Critical Cellular Functions and Mechanisms of Action of the RNA Helicase UAP56.Journal of molecular biology · 2024Review
- Identification of ALYREF in pan cancer as a novel cancer prognostic biomarker and potential regulatory mechanism in gastric cancer.Scientific reports · 2024Article
- TREX tetramer disruption alters RNA processing necessary for corticogenesis in THOC6 Intellectual Disability Syndrome.Nature communications · 2024Article
- Structural differences between the closely related RNA helicases, UAP56 and URH49, fashion distinct functional apo-complexes.Nature communications · 2024Article
- Single-molecule quantitation of RNA-binding protein occupancy and stoichiometry defines a role for Yra1 (Aly/REF) in nuclear mRNP organization.Cell reports · 2023Article
- Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023Review
- Nuclear mRNPs are compact particles packaged with a network of proteins promoting RNA-RNA interactions.Genes & development · 2023Article
- Article
- DDX39B drives colorectal cancer progression by promoting the stability and nuclear translocation of PKM2.Signal transduction and targeted therapy · 2022Article
- Nuclear mRNA maturation and mRNA export control: from trypanosomes to opisthokonts.Parasitology · 2021Review
- The DDX39B/FUT3/TGFβR-I axis promotes tumor metastasis and EMT in colorectal cancer.Cell death & disease · 2021Article
- TPR is required for the efficient nuclear export of mRNAs and lncRNAs from short and intron-poor genes.Nucleic acids research · 2020Article
- Structure of the human core transcription-export complex reveals a hub for multivalent interactions.eLife · 2020Article
- Cellular mRNA export factor UAP56 recognizes nucleic acid binding site of influenza virus NP protein.Biochemical and biophysical research communications · 2020Article
8 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
No grant is acknowledged in the PubMed record.
Abstract
Loading of export factors onto mRNAs is a key step in gene expression. In vertebrates, splicing plays a role in this process. Specific protein complexes, exon junction complex and transcription/export complex, are loaded onto mRNAs in a splicing-dependent manner, and adaptor proteins such as Aly/REF in the complexes in turn recruit mRNA exporter TAP-p15 onto the RNA. By contrast, how export factors are recruited onto intronless mRNAs is largely unknown. We previously showed that Aly/REF is preferentially associated with intronless mRNAs in the nucleus. Here we show that Aly/REF could preferentially bind intronless mRNAs in vitro and that this binding was stimulated by RNA helicase UAP56 in an ATP-dependent manner. Consistently, an ATP binding-deficient UAP56 mutant specifically inhibited mRNA export in Xenopus oocytes. Interestingly, ATP activated the RNA binding activity of UAP56 itself. ATP-bound UAP56 therefore bound to both RNA and Aly/REF, and as a result ATPase activity of UAP56 was cooperatively stimulated. These results are consistent with a model in which ATP-bound UAP56 chaperones Aly/REF onto RNA, ATP is then hydrolyzed, and UAP56 dissociates from RNA for the next round of Aly/REF recruitment. Our finding provides a mechanistic insight into how export factors are recruited onto mRNAs.
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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.