ArticleStructure (London, England : 1993)2015
Structural Characterization of the Chaetomium thermophilum TREX-2 Complex and its Interaction with the mRNA Nuclear Export Factor Mex67:Mtr2.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
19 citing papers in PubMed, 35 citations in OpenAlex.
- Molecular insights into mRNA export regulation by the human TREX-2 complex.Nature communications · 2026Article
- Article
- Unraveling gene expression: a beginner's guide from chromatin modifications to mRNA export inNucleus (Austin, Tex.) · 2025Review
- Structural mechanism of DDX39B regulation by human TREX-2 and a related complex in mRNP remodeling.Nature communications · 2025Article
- Article
- TREX-2-ORC Complex of D. melanogaster Participates in Nuclear Export of Histone mRNA.Doklady. Biochemistry and biophysics · 2024Article
- The Human TREX-2 Complex Interacts with Subunits of the ORC Complex.Doklady. Biochemistry and biophysics · 2023Article
- Nuclear transport proteins: structure, function, and disease relevance.Signal transduction and targeted therapy · 2023Review
- A Protein-Protein Interaction Analysis Suggests a Wide Range of New Functions for the p21-Activated Kinase (PAK) Ste20.International journal of molecular sciences · 2023Article
- PCID2 Subunit of theCurrent issues in molecular biology · 2023Article
- Validation and classification of RNA binding proteins identified by mRNA interactome capture.RNA (New York, N.Y.) · 2021Article
- Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021Review
- Mechanisms of nuclear mRNA export: A structural perspective.Traffic (Copenhagen, Denmark) · 2019Review
- Article
- Structure of the Sac3 RNA-binding M-region in the Saccharomyces cerevisiae TREX-2 complex.Nucleic acids research · 2017Article
- Interaction network of the ribosome assembly machinery from a eukaryotic thermophile.Protein science : a publication of the Protein Society · 2017Article
- The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region.Journal of structural biology · 2016Article
- Mediator and TREX-2: Emerging links between transcription initiation and mRNA export.Nucleus (Austin, Tex.) · 2016Article
- 1.25 Å resolution structure of an RNA 20-mer that binds to the TREX2 complex.Acta crystallographica. Section F, Structural biology communications · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
The TREX-2 complex integrates mRNA nuclear export into the gene expression pathway and is based on a Sac3 scaffold to which Thp1, Sem1, Sus1, and Cdc31 bind. TREX-2 also binds the mRNA nuclear export factor, Mex67:Mtr2, through the Sac3 N-terminal region (Sac3N). Here, we characterize Chaetomium thermophilum TREX-2, show that the in vitro reconstituted complex has an annular structure, and define the structural basis for interactions between Sac3, Sus1, Cdc31, and Mex67:Mtr2. Crystal structures show that the binding of C. thermophilum Sac3N to the Mex67 NTF2-like domain (Mex67(NTF2L)) is mediated primarily through phenylalanine residues present in a series of repeating sequence motifs that resemble those seen in many nucleoporins, and Mlp1 also binds Mex67:Mtr2 using a similar motif. Deletion of Sac3N generated growth and mRNA export defects in Saccharomyces cerevisiae, and we propose TREX-2 and Mlp1 function to facilitate export by concentrating mature messenger ribonucleoparticles at the nuclear pore entrance.
Indexed as
Identifiers
What OpenQuestion holds
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.