Evidence map›Paper›PMID 22090346›Full record

ArticleMolecular biology of the cell2012

RNA-related nuclear functions of human Pat1b, the P-body mRNA decay factor.

Aline Marnef, Dominique Weil, Nancy Standart

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
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  4. Article
  5. DNA topoisomerase 2-associated proteins PATL1 and PATL2 regulate the biogenesis of hERG KProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  8. Review
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  12. The sole LSm complex inRNA (New York, N.Y.) · 2017
    Article
  13. Article
  14. Article
  15. Multifaceted Roles of ALG-2 in Ca(2+)-Regulated Membrane Trafficking.International journal of molecular sciences · 2016
    Review
  16. Article
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  18. Article
  19. 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

3 authors at 2 institutions in 2 countries.

Aline MarnefDepartment of Biochemistry, University of Cambridge, Cambridge, United Kingdom.
Dominique Weil
Nancy Standart
University of Cambridge · GBCentre National de la Recherche Scientifique · FR

Funding

Biotechnology and Biological Sciences Research CouncilWellcome Trust
6 · The paper itself

Abstract

The evolutionarily conserved Pat1 proteins are P-body components recently shown to play important roles in cytoplasmic gene expression control. Using human cell lines, we demonstrate that human Pat1b is a shuttling protein whose nuclear export is mediated via a consensus NES sequence and Crm1, as evidenced by leptomycin B (LMB) treatment. However, not all P-body components are nucleocytoplasmic proteins; rck/p54, Dcp1a, Edc3, Ge-1, and Xrn1 are insensitive to LMB and remain cytoplasmic in its presence. Nuclear Pat1b localizes to PML-associated foci and SC35-containing splicing speckles in a transcription-dependent manner, whereas in the absence of RNA synthesis, Pat1b redistributes to crescent-shaped nucleolar caps. Furthermore, inhibition of splicing by spliceostatin A leads to the reorganization of SC35 speckles, which is closely mirrored by Pat1b, indicating that it may also be involved in splicing processes. Of interest, Pat1b retention in these three nuclear compartments is mediated via distinct regions of the protein. Examination of the nuclear distribution of 4E-T(ransporter), an additional P-body nucleocytoplasmic protein, revealed that 4E-T colocalizes with Pat1b in PML-associated foci but not in nucleolar caps. Taken together, our findings strongly suggest that Pat1b participates in several RNA-related nuclear processes in addition to its multiple regulatory roles in the cytoplasm.

Indexed as

RNA Processing, Post-TranscriptionalRNA StabilityActive Transport, Cell NucleusAmino Acid SequenceAmino Acid SubstitutionCell LineCell NucleusDNA-Binding ProteinsGene Expression RegulationHumansMolecular Sequence DataMutagenesis, Site-DirectedNuclear Export SignalsNuclear Localization SignalsNucleocytoplasmic Transport ProteinsProtein BindingDNA-Binding ProteinsEIF4ENIF1 protein, humanNuclear Export SignalsNuclear Localization SignalsNucleocytoplasmic Transport ProteinsPATL1 protein, humanRNA, Messenger

Identifiers

PMID22090346
PMCPMC3248899
OpenAlexW2041750884

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.