Evidence map›Paper›PMID 25378478›Full record

ArticleThe EMBO journal2014

The mammalian tRNA ligase complex mediates splicing of XBP1 mRNA and controls antibody secretion in plasma cells.

Jennifer Jurkin, Theresa Henkel, Anne Færch Nielsen, Martina Minnich, Johannes Popow, Therese Kaufmann, Katrin Heindl, Thomas Hoffmann, Meinrad Busslinger, Javier Martinez

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.

0numbers the graph read from it
0cells of the map it votes in
140citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

140 citing papers in PubMed, 211 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Metabolites · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026
    Review
  10. RNase L Regulates Antiviral Responsiveness through Cleavage of XBP1 mRNA.bioRxiv : the preprint server for biology · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 6 institutions in 3 countries.

Jennifer JurkinInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Theresa HenkelInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Anne Færch NielsenEuropean Molecular Biology Organization (EMBO), Heidelberg, Germany.
Martina MinnichInstitute of Molecular Pathology (IMP), Vienna, Austria.
Johannes PopowEuropean Molecular Biology Laboratory (EMBL), Heidelberg, Germany.
Therese KaufmannInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria.
Katrin HeindlWhitehead Institute for Biomedical Research, Cambridge, MA, USA.
Thomas HoffmannInstitute of Molecular Pathology (IMP), Vienna, Austria.
Meinrad BusslingerInstitute of Molecular Pathology (IMP), Vienna, Austria.
Javier MartinezInstitute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA), Vienna, Austria javier.martinez@imba.oeaw.ac.at.
Austrian Academy of Sciences · ATResearch Institute of Molecular Pathology · ATEuropean Molecular Biology Laboratory · DEEuropean Molecular Biology Organization · DEInstitute of Molecular Biotechnology · ATWhitehead Institute for Biomedical Research · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The unfolded protein response (UPR) is a conserved stress-signaling pathway activated after accumulation of unfolded proteins within the endoplasmic reticulum (ER). Active UPR signaling leads to unconventional, enzymatic splicing of XBP1 mRNA enabling expression of the transcription factor XBP1s to control ER homeostasis. While IRE1 has been identified as the endoribonuclease required for cleavage of this mRNA, the corresponding ligase in mammalian cells has remained elusive. Here, we report that RTCB, the catalytic subunit of the tRNA ligase complex, and its co-factor archease mediate XBP1 mRNA splicing both in vitro and in vivo. Depletion of RTCB in plasma cells of Rtcb(fl/fl) Cd23-Cre mice prevents XBP1s expression, which normally is strongly induced during plasma cell development. RTCB-depleted plasma cells show reduced and disorganized ER structures as well as severe defects in antibody secretion. Targeting RTCB and/or archease thus represents a promising strategy for the treatment of a growing number of diseases associated with elevated expression of XBP1s.

Indexed as

RNA SplicingAmino Acyl-tRNA SynthetasesAnimalsAntibodiesDNA-Binding ProteinsHeLa CellsHumansMicePlasma CellsProteinsRegulatory Factor X Transcription FactorsRNA-Binding ProteinsRNA, MessengerTranscription FactorsX-Box Binding Protein 1Amino Acyl-tRNA SynthetasesAntibodiesDNA-Binding ProteinsFAAP protein, mouseProteinsRegulatory Factor X Transcription FactorsRNA-Binding ProteinsRNA, MessengerTranscription FactorsX-Box Binding Protein 1XBP1 protein, humanXbp1 protein, mouseZBTB8OS protein, humanantibody secretionarcheaseplasma cellsRTCBXBP1 mRNA splicing

Identifiers

PMID25378478
PMCPMC4282640
OpenAlexW2130241868

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.