Evidence map›Paper›PMID 12515382›Full record

ArticleRNA (New York, N.Y.)2002

The human LSm1-7 proteins colocalize with the mRNA-degrading enzymes Dcp1/2 and Xrnl in distinct cytoplasmic foci.

Dierk Ingelfinger, Donna J Arndt-Jovin, Reinhard Lührmann, Tilmann Achsel

Open access · greenAbstract read
In one paragraph

Article in RNA (New York, N.Y.), 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 219 papers.

0numbers the graph read from it
0cells of the map it votes in
219citing papers in PubMed
8.2field-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

219 citing papers in PubMed, 397 citations in OpenAlex.

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  13. A closer look at mammalian antiviral condensates.Biochemical Society transactions · 2024
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  17. Germ Granules in Animal Oogenesis.Journal of developmental biology · 2022
    Review
  18. Article
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  20. Article

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

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

4 authors at 1 institution in 2 countries.

Dierk IngelfingerDepartment of Cellular Biochemistry, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany.
Donna J Arndt-Jovin
Reinhard Lührmann
Tilmann Achsel
Max Planck Institute for Biophysical Chemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sm and Sm-like (LSm) proteins form heptameric complexes that are involved in various steps of RNA metabolism. In yeast, the Lsm1-7 complex functions in mRNA degradation and is associated with several enzymes of this pathway, while the complex LSm2-8, the composition of which largely overlaps with that of LSm1-7, has a role in pre-mRNA splicing. A human gene encoding an LSm1 homolog has been identified, but its role in mRNA degradation has yet to be elucidated. We performed subcellular localization studies and found hLSm1 predominantly in the cytoplasm. However, it is not distributed evenly; rather, it is highly enriched in small, discrete foci. The endogenous hLSm4 is similarly localized, as are the overexpressed proteins hLSm1-7, but not hLSm8. The foci also contain two key factors in mRNA degradation, namely the decapping enzyme hDcp1/2 and the exonuclease hXrn1. Moreover, coexpression of wild-type and mutant LSm proteins, as well as fluorescence resonance energy transfer (FRET) studies, indicate that the mammalian proteins hLSm1-7 form a complex similar to the one found in yeast, and that complex formation is required for enrichment of the proteins in the cytoplasmic foci. Therefore, the foci contain a partially or fully assembled machinery for the degradation of mRNA.

Indexed as

RNA-Binding ProteinsSaccharomyces cerevisiae ProteinsCytoplasmEndoribonucleasesExoribonucleasesFungal ProteinsHeLa CellsHumansMacromolecular SubstancesMicrotubule-Associated ProteinsN-Terminal Acetyltransferase CRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA Cap-Binding ProteinsRNA, MessengerDCP1 protein, S cerevisiaeDCP2 protein, humanEndoribonucleasesExoribonucleasesFungal ProteinsMacromolecular SubstancesMicrotubule-Associated ProteinsNAA38 protein, humanN-Terminal Acetyltransferase CRibonucleoproteins, Small NuclearRibonucleoprotein, U4-U6 Small NuclearRNA-Binding ProteinsRNA Cap-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae ProteinsXRN1 protein, human

Identifiers

PMID12515382
PMCPMC1370355
OpenAlexW2136615690

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.