Evidence map›Paper›PMID 25838545›Full record

ArticleGenes & development2015

In vivo biochemical analyses reveal distinct roles of β-importins and eEF1A in tRNA subcellular traffic.

Hsiao-Yun Huang, Anita K Hopper

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
–field-weighted citation impact
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

32 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Gle1 is required for tRNA to stimulate Dbp5 ATPase activitybioRxiv : the preprint server for biology · 2023
    Article
  6. The life and times of a tRNA.RNA (New York, N.Y.) · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. tRNA Metabolism and Neurodevelopmental Disorders.Annual review of genomics and human genetics · 2019
    Review
  18. Article
  19. Article
  20. Review
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

2 authors at 1 institution in 1 country.

Hsiao-Yun HuangDepartment of Molecular Genetics, Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA.
Anita K HopperDepartment of Molecular Genetics, Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA hopper.64@osu.edu.
The Ohio State University · US

Funding

YEAST GENES IN RNA PROCESSING &NUCLEUS/CYTOSOL EXCHANGER01GM027930 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI HOPPER, ANITA K · 1985 to 2014
$4.6M
NIGMS NIH HHS GM27930NIGMS NIH HHS R01 GM027930
6 · The paper itself

Abstract

Bidirectional tRNA movement between the nucleus and the cytoplasm serves multiple biological functions. To gain a biochemical understanding of the mechanisms for tRNA subcellular dynamics, we developed in vivo β-importin complex coimmunoprecipitation (co-IP) assays using budding yeast. Our studies provide the first in vivo biochemical evidence that two β-importin family members, Los1 (exportin-t) and Msn5 (exportin-5), serve overlapping but distinct roles in tRNA nuclear export. Los1 assembles complexes with RanGTP and tRNA. Both intron-containing pre-tRNAs and spliced tRNAs, regardless of whether they are aminoacylated, assemble into Los1-RanGTP complexes, documenting that Los1 participates in both primary nuclear export and re-export of tRNAs to the cytoplasm. In contrast, β-importin Msn5 preferentially assembles with RanGTP and spliced, aminoacylated tRNAs, documenting its role in tRNA nuclear re-export. Tef1/2 (the yeast form of translation elongation factor 1α [eEF1A]) aids the specificity of Msn5 for aminoacylated tRNAs to form a quaternary complex consisting of Msn5, RanGTP, aminoacylated tRNA, and Tef1/2. Assembly and/or stability of this quaternary complex requires Tef1/2, thereby facilitating efficient re-export of aminoacylated tRNAs to the cytoplasm.

Indexed as

Active Transport, Cell Nucleusbeta KaryopherinsCell NucleusCytoplasmEukaryotic Initiation FactorsKaryopherinsNucleocytoplasmic Transport ProteinsPeptide Elongation Factor 1Peptide Elongation FactorsProtein Structure, QuaternaryRNA-Binding ProteinsRNA, TransferSaccharomyces cerevisiaeSaccharomyces cerevisiae Proteinsbeta KaryopherinsEukaryotic Initiation FactorsKaryopherinsMSN5 protein, S cerevisiaeMTR10 protein, S cerevisiaeNucleocytoplasmic Transport ProteinsPeptide Elongation Factor 1Peptide Elongation FactorsRNA-Binding ProteinsRNA, TransferSaccharomyces cerevisiae ProteinsTEF1 protein, S cerevisiaeTEF2 protein, S cerevisiaeLos1Msn5Mtr10nuclear exportSaccharomyces cerevisiaeTef1/2

Identifiers

PMID25838545
PMCPMC4387718
OpenAlexW2026102786

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.