ArticleThe EMBO journal2002
The mRNA export factor Dbp5 is associated with Balbiani ring mRNP from gene to cytoplasm.
Article in The EMBO journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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.
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Who cites it
50 citing papers in PubMed, 118 citations in OpenAlex.
- Article
- Gle1 is required for tRNA to stimulate Dbp5 ATPase activitybioRxiv : the preprint server for biology · 2023Article
- RNA export through the nuclear pore complex is directional.Nature communications · 2022Article
- Imaging Organization of RNA Processing within the Nucleus.Cold Spring Harbor perspectives in biology · 2021Review
- Emerging molecular functions and novel roles for the DEAD-box protein Dbp5/DDX19 in gene expression.Cellular and molecular life sciences : CMLS · 2021Review
- Dbp5 associates with RNA-bound Mex67 and Nab2 and its localization at the nuclear pore complex is sufficient for mRNP export and cell viability.PLoS genetics · 2020Article
- Dbp5/DDX19 between Translational Readthrough and Nonsense Mediated Decay.International journal of molecular sciences · 2020Review
- The RNA export factor Mex67 functions as a mobile nucleoporin.The Journal of cell biology · 2019Article
- Article
- Ddx19 links mRNA nuclear export with progression of transcription and replication and suppresses genomic instability upon DNA damage in proliferating cells.Nucleus (Austin, Tex.) · 2017Review
- RNA helicase DDX19 stabilizes ribosomal elongation and termination complexes.Nucleic acids research · 2017Article
- Temporal and spatial regulation of mRNA export: Single particle RNA-imaging provides new tools and insights.BioEssays : news and reviews in molecular, cellular and developmental biology · 2017Review
- Influenza A Virus Polymerase Recruits the RNA Helicase DDX19 to Promote the Nuclear Export of Viral mRNAs.Scientific reports · 2016Article
- P(I) Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5).Journal of molecular biology · 2016Article
- RNA export factor Ddx19 is required for nuclear import of the SRF coactivator MKL1.Nature communications · 2015Article
- High-resolution imaging reveals new features of nuclear export of mRNA through the nuclear pore complexes.International journal of molecular sciences · 2014Review
- Insights into mRNP biogenesis provided by new genetic interactions among export and transcription factors.BMC genetics · 2012Article
- Nuclear export of single native mRNA molecules observed by light sheet fluorescence microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- To the pore and through the pore: a story of mRNA export kinetics.Biochimica et biophysica acta · 2012Review
- From unwinding to clamping - the DEAD box RNA helicase family.Nature reviews. Molecular cell biology · 2011Review
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The DEAD box RNA helicase Dbp5 is essential for nucleocytoplasmic transport of mRNA-protein (mRNP) complexes. Dbp5 is present mainly in the cytoplasm and is enriched at the cytoplasmic side of nuclear pore complexes (NPCs), suggesting that it acts in the late part of mRNP export. Here, we visualize the assembly and transport of a specific mRNP particle, the Balbiani ring mRNP in the dipteran Chironomus tentans, and show that a Dbp5 homologue in C.tentans, Ct-Dbp5, binds to pre-mRNP co-transcriptionally and accompanies the mRNP to and through the nuclear pores and into the cytoplasm. We also demonstrate that Ct-Dbp5 accumulates in the nucleus and partly disappears from the NPC when nuclear export of mRNA is inhibited. The fact that Ct-Dbp5 is present along the exiting mRNP fibril extending from the nuclear pore into the cytoplasm supports the view that Ct-Dbp5 is involved in restructuring the mRNP prior to translation. Finally, the addition of the export factor Dbp5 to the growing transcript highlights the importance of the co-transcriptional loading process in determining the fate of mRNA.
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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.