Evidence map›Paper›PMID 22353712›Full record

ArticleNature communications2012

Unique domain appended to vertebrate tRNA synthetase is essential for vascular development.

Xiaoling Xu, Yi Shi, Hui-Min Zhang, Eric C Swindell, Alan G Marshall, Min Guo, Shuji Kishi, Xiang-Lei Yang

Open access · hybridAbstract read
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.

0numbers the graph read from it
0cells of the map it votes in
61citing papers in PubMed
4.0field-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

61 citing papers in PubMed, 105 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Structural basis of tRNA recognition by the mNature structural & molecular biology · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Multi-omic stratification of the missense variant cysteinome.bioRxiv : the preprint server for biology · 2023
    Article
  10. Review
  11. Article
  12. Loss of seryl-tRNA synthetase (Journal of medical genetics · 2022
    Article
  13. Article
  14. Article
  15. Self-transducible LRS-UNE-L peptide enhances muscle regeneration.Journal of cachexia, sarcopenia and muscle · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Translational control in aging and neurodegeneration.Wiley interdisciplinary reviews. RNA · 2021
    Review

1 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 1 country.

Xiaoling XuDepartment of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA.
Yi Shi
Hui-Min Zhang
Eric C Swindell
Alan G Marshall
Min Guo
Shuji Kishi
Xiang-Lei Yang
Scripps Research Institute · USNational High Magnetic Field Laboratory · USThe University of Texas Health Science Center at Houston · US

Funding

GENETIC APPROACHES TO PROTEIN/NUCLEIC ACID INTERACTIONSR01GM023562 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SCHIMMEL, PAUL R · 1985 to 2012
$4.9M
Extra-translational roles of aminoacyl tRNA synthetases in connection to diseaseR01GM088278 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI YANG, XIANG-LEI · 2010 to 2019
$3.7M
Structural Mapping of Protein Complexes by Hydrogen/Deuterium ExchangeR01GM078359 · NIGMS · FLORIDA STATE UNIVERSITY · PI MARSHALL, ALAN G · 2006 to 2009
$1.2M
NCRR NIH HHS U54 RR025204NIGMS NIH HHS GM 23562NIGMS NIH HHS GM 78359NIGMS NIH HHS GM88278NIGMS NIH HHS R01 GM023562NIGMS NIH HHS R01 GM078359NIGMS NIH HHS R01 GM088278
6 · The paper itself

Abstract

New domains were progressively added to cytoplasmic aminoacyl transfer RNA (tRNA) synthetases during evolution. One example is the UNE-S domain, appended to seryl-tRNA synthetase (SerRS) in species that developed closed circulatory systems. Here we show using solution and crystal structure analyses and in vitro and in vivo functional studies that UNE-S harbours a robust nuclear localization signal (NLS) directing SerRS to the nucleus where it attenuates vascular endothelial growth factor A expression. We also show that SerRS mutants previously linked to vasculature abnormalities either deleted the NLS or have the NLS sequestered in an alternative conformation. A structure-based second-site mutation, designed to release the sequestered NLS, restored normal vasculature. Thus, the essential function of SerRS in vascular development depends on UNE-S. These results are the first to show an essential role for a tRNA synthetase-associated appended domain at the organism level, and suggest that acquisition of UNE-S has a role in the establishment of the closed circulatory systems of vertebrates.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceAminoacylationAnimalsBlood VesselsCell NucleusCrystallography, X-RayHumansMolecular Sequence DataMutationNeovascularization, PhysiologicNuclear Localization SignalsProtein ConformationProtein Structure, SecondaryProtein Structure, TertiarySerine-tRNA LigaseNuclear Localization SignalsSerine-tRNA LigaseVascular Endothelial Growth Factor AZebrafish Proteins

Identifiers

PMID22353712
PMCPMC3293412
OpenAlexW2100534662

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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 OpenQuestion graph.