Evidence map›Paper›PMID 21522132›Full record

ArticleThe EMBO journal2011

CRM1 controls the composition of nucleoplasmic pre-snoRNA complexes to licence them for nucleolar transport.

Bérengère Pradet-Balade, Cyrille Girard, Séverine Boulon, Conception Paul, Karim Azzag, Rémy Bordonné, Edouard Bertrand, Céline Verheggen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 46 citations in OpenAlex.

  1. Biogenesis and Regulation of Telomerase during Development and Cancer.Cold Spring Harbor perspectives in biology · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
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  7. Article
  8. The roles of NOP56 in cancer and SCA36.Pathology oncology research : POR · 2023
    Review
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  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
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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

8 authors at 3 institutions in 1 country.

Bérengère Pradet-BaladeInstitut de Génétique Moléculaire de Montpellier, UMR 5535 CNRS, Université Montpellier I and II, Montpellier Cedex 5, France.
Cyrille Girard
Séverine Boulon
Conception Paul
Karim Azzag
Rémy Bordonné
Edouard Bertrand
Céline Verheggen
Institut de Génétique Moléculaire de Montpellier · FRUniversité de Montpellier · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transport of C/D snoRNPs to nucleoli involves nuclear export factors. In particular, CRM1 binds nascent snoRNPs, but its precise role remains unknown. We show here that both CRM1 and nucleocytoplasmic trafficking are required to transport snoRNPs to nucleoli, but the snoRNPs do not transit through the cytoplasm. Instead, CRM1 controls the composition of nucleoplasmic pre-snoRNP complexes. We observed that Tgs1 long form (Tgs1 LF), the long isoform of the cap hypermethylase, contains a leucine-rich nuclear export signal, shuttles in a CRM1-dependent manner, and binds to the nucleolar localization signal (NoLS) of the core snoRNP protein Nop58. In vitro data indicate that CRM1 binds Tgs1 LF and promotes its dissociation from Nop58 NoLS, and immunoprecipitation experiments from cells indicate that the association of Tgs1 LF with snoRNPs increases upon CRM1 inhibition. Thus, CRM1 appears to promote nucleolar transport of snoRNPs by removing Tgs1 LF from the Nop58 NoLS. Microarray/IP data show that this occurs on most snoRNPs, from both C/D and H/ACA families, and on the telomerase RNA. Hence, CRM1 provides a general molecular link between nuclear events and nucleocytoplasmic trafficking.

Indexed as

Active Transport, Cell NucleusCell LineCell NucleusExportin 1 ProteinHumansKaryopherinsMethyltransferasesNuclear ProteinsProtein BindingReceptors, Cytoplasmic and NuclearRibonucleoproteins, Small NucleolarRNA, Small NucleolarExportin 1 ProteinKaryopherinsMethyltransferasesNOP58 protein, humanNuclear ProteinsReceptors, Cytoplasmic and NuclearRibonucleoproteins, Small NucleolarRNA, Small Nucleolartrimethylguanosine synthase

Identifiers

PMID21522132
PMCPMC3117649
OpenAlexW1775357008

What OpenQuestion holds

Textmetadata
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.