Evidence map›Paper›PMID 37578863›Full record

ArticleCell reports2023

Structural basis for high-order complex of SARNP and DDX39B to facilitate mRNP assembly.

Yihu Xie, Shengyan Gao, Ke Zhang, Prasanna Bhat, Bradley P Clarke, Kimberly Batten, Menghan Mei, Matthew Gazzara, Jerry W Shay, Kristen W Lynch and 5 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  8. Review
  9. Article
  10. Structures and mRNP remodeling mechanism of the TREX-2 complex.Structure (London, England : 1993) · 2025
    Article
  11. Article
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  14. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 4 institutions in 1 country.

Yihu XieDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Shengyan GaoDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.
Ke ZhangDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.
Prasanna BhatDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.
Bradley P ClarkeDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Kimberly BattenDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.
Menghan MeiDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Matthew GazzaraDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.
Jerry W ShayDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.
Kristen W LynchDepartment of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA.
Alexia E AngelosDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Pate S HillDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Austin L IveyDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Beatriz M A FontouraDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA. Electronic address: beatriz.fontoura@utsouthwestern.edu.
Yi RenDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA; Center for Structural Biology, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA. Electronic address: yi.ren@vanderbilt.edu.
Vanderbilt University · USThe University of Texas Southwestern Medical Center · USUniversity of Pennsylvania · USSouthwestern Medical Center · US

Funding

Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
Signal-Induced Regulation of Alternative RNA ProcessingR35GM118048 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KRISTEN W LYNCH · 2016 to 2026
$6.6M
Splicing and Nuclear Transport of Influenza Virus mRNAR01AI125524 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI COBB, MELANIE H., FONTOURA, BEATRIZ MA · 2016 to 2025
$5.6M
Virulence Factor at the Interface of Viral and Cellular mRNA Nuclear ExportR01AI154635 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI Beatriz MA Fontoura · 2020 to 2026
$5.1M
Mechanisms and Regulation of Nuclear mRNA ExportR35GM133743 · NIGMS · VANDERBILT UNIVERSITY · PI Yi Ren · 2019 to 2026
$3.6M
Mechanisms and consequences of 3'UTR isoform diversity in erythropoiesisF31HL162546 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI GAZZARA, MATTHEW ROBERT · 2022 to 2024
$136k
NCI NIH HHS T32 CA119925NHLBI NIH HHS F31 HL162546NIAID NIH HHS R01 AI125524NIAID NIH HHS R01 AI154635NIGMS NIH HHS R35 GM118048NIGMS NIH HHS R35 GM133743
6 · The paper itself

Abstract

mRNA in eukaryotic cells is packaged into highly compacted ribonucleoprotein particles (mRNPs) in the nucleus and exported to the cytoplasm for translation. mRNP packaging and export require the evolutionarily conserved transcription-export (TREX) complex. TREX facilitates loading of various RNA-binding proteins on mRNA through the action of its DDX39B subunit. SARNP (Tho1 [transcriptional defect of Hpr1 by overexpression 1] in yeast) is shown to interact with DDX39B and affect mRNA export. The molecular mechanism of how SARNP recognizes DDX39B and functions in mRNP assembly is unclear. Here, we determine the crystal structure of a Tho1/DDX39B/RNA complex, revealing a multivalent interaction mediated by tandem DDX39B interacting motifs in SARNP/Tho1. The high-order complex of SARNP and DDX39B is evolutionarily conserved, and human SARNP can engage with five DDX39B molecules. RNA sequencing (RNA-seq) from SARNP knockdown cells shows the most affected RNAs in export are GC rich. Our work suggests the role of the high-order SARNP/DDX39B/RNA complex in mRNP assembly and export.

Indexed as

Nuclear ProteinsRibonucleoproteinsDEAD-box RNA HelicasesHumansRNA, MessengerSaccharomyces cerevisiaeTranscription FactorsDDX39B protein, humanDEAD-box RNA Helicasesmessenger ribonucleoproteinNuclear ProteinsRibonucleoproteinsRNA, MessengerSARNP protein, humanTranscription FactorsCP: Molecular biologyDDX39BDEAD-box ATPasemRNA nuclear exportmRNP assemblySARNPSub2Tho1TREX complexUAP56

Identifiers

PMID37578863
PMCPMC10508174
OpenAlexW4385813626

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

None linked

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 Socratic graph.