ArticleStructure (London, England : 1993)2025
Structures and mRNP remodeling mechanism of the TREX-2 complex.
Article in Structure (London, England : 1993), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Conserved mRNP remodeling mechanism of the TREX-2.1 complex.Nucleic acids research · 2026Article
- Mechanisms of transcription termination across the coding and noncoding loci of the genome.Nature reviews. Molecular cell biology · 2026Review
- Evolutionarily conserved spliceosome-exosome pathway in nuclear mRNA surveillance.Genes & development · 2026Article
- Article
- Escorting mRNAs - the multifunctional and divergent roles of cap-chaperones in post-transcriptional gene expression.Journal of cell science · 2026Review
- LENG8 mediates RNA nuclear retention and degradation in eukaryotes.Molecular cell · 2026Article
- TREX2 component PCID2 scaffolds alternative SAC3-based subcomplexes with distinct RNA processing and export function.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
- Article
- Viral interference of nucleocytoplasmic transport.The Journal of biological chemistry · 2025Review
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- From transcription to export: mRNA's winding path to the cytoplasm.Trends in biochemical sciences · 2025Review
- Identification of divergentbioRxiv : the preprint server for biology · 2025Article
- A time-resolved framework for the recruitment of mRNP processing and assembly factors to a site of transcription.Nucleic acids research · 2025Article
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Mixed Messages: Dynamic and Compositional Heterogeneity of Nuclear Messenger Ribonucleoprotein (mRNP) Complexes.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
15 authors.
Funding
Abstract
mRNAs are packaged with proteins into messenger ribonucleoprotein complexes (mRNPs) in the nucleus. mRNP assembly and export are of fundamental importance for all eukaryotic gene expression. Before export to the cytoplasm, mRNPs undergo dynamic remodeling governed by the DEAD-box helicase DDX39B (yeast Sub2). DDX39B/Sub2 primarily functions in the nucleus and leaves the mRNP prior to export through the nuclear pore complex; however, the underlying mechanisms remain elusive. Here, we identify the conserved TREX-2 complex as the long-sought factor that facilitates DDX39B/Sub2 to complete the mRNP remodeling cycle. Our crystallographic and cryoelectron microscopy (cryo-EM) analyses demonstrate that TREX-2 modulates the activities of DDX39B/Sub2 through multiple interactions. Critically, a conserved "trigger loop" from TREX-2 splits the two RecA domains of DDX39B/Sub2 and promotes the removal of DDX39B/Sub2 from mRNP. Our findings suggest that TREX-2 coordinates with DDX39B/Sub2 and the human export receptor NXF1-NXT1 (yeast Mex67-Mtr2) to complete the final steps of nuclear mRNP assembly.
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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.