Evidence map›Paper›PMID 22244335›Full record

ArticleMolecular cell2012

H2B ubiquitylation controls the formation of export-competent mRNP.

Adeline Vitaliano-Prunier, Anna Babour, Lucas Hérissant, Luciano Apponi, Thanasis Margaritis, Frank C P Holstege, Anita H Corbett, Carole Gwizdek, Catherine Dargemont

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

  1. Decoding RNF20: an epigenetic modifier and beyond.Frontiers in cell and developmental biology · 2026
    Review
  2. Article
  3. Review
  4. Nuclear mRNA export.Acta biochimica et biophysica Sinica · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Review
  18. Article
  19. Monoubiquitylation of histone H2B contributes to the bypass of DNA damage during and after DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Article
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

9 authors at 2 institutions in 2 countries.

Adeline Vitaliano-PrunierInstitut Jacques Monod, Université Paris Diderot, CNRS, Bâtiment Buffon, 15 rue Hélène Brion, 75205 Paris Cedex 13, France.
Anna Babour
Lucas Hérissant
Luciano Apponi
Thanasis Margaritis
Frank C P Holstege
Anita H Corbett
Carole Gwizdek
Catherine Dargemont
Emory University · USUtrecht University · NL

Funding

MOLECULAR BASIS OF RAN MEDIATED NUCLEAR TRANSPORTR01GM058728 · NIGMS · EMORY UNIVERSITY · PI CORBETT, ANITA H. · 1999 to 2016
$5.4M
NIGMS NIH HHS R01 GM058728
6 · The paper itself

Abstract

Histone H2B ubiquitylation is a transcription-dependent modification that not only regulates nucleosome dynamics but also controls the trimethylation of histone H3 on lysine 4 by promoting ubiquitylation of Swd2, a component of both the histone methyltransferase COMPASS complex and the cleavage and polyadenylation factor(CPF). We show that preventing either H2B ubiquitylation or H2B-dependent modification of Swd2 results in nuclear accumulation of poly(A) RNA due to a defect in the integrity and stability of APT, a subcomplex of the CPF. Ubiquitin-regulated APT complex dynamics is required for the correct recruitment of the mRNA export receptor Mex67 to nuclear mRNPs. While H2B ubiquitylation controls the recruitment of the different Mex67 adaptors to mRNPs, the effect of Swd2 ubiquitylation is restricted to Yra1 and Nab2, which, in turn, controls poly(A) tail length. Modification of H2B thus participates in the crosstalk between cotranscriptional events and assembly of mRNPs linking nuclear processing and mRNA export.

Indexed as

UbiquitinationActive Transport, Cell NucleusCell NucleusHistone-Lysine N-MethyltransferaseHistonesNuclear ProteinsNucleocytoplasmic Transport ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHistone-Lysine N-MethyltransferaseHistonesmessenger ribonucleoproteinNAB2 protein, S cerevisiaeNuclear ProteinsNucleocytoplasmic Transport ProteinsRibonucleoproteinsRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsSWD2 protein, S cerevisiaeYRA1 protein, S cerevisiae

Identifiers

PMID22244335
PMCPMC3259529
OpenAlexW1993512472

What OpenQuestion holds

Textmetadata
LicenceTDM
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.