Evidence map›Paper›PMID 23885126›Full record

ArticleMolecular biology of the cell2013

Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/importin-7 in snRNP biogenesis.

Amanda Hicks Natalizio, A Gregory Matera

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 34% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Article
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  5. Article
  6. Review
  7. Article
  8. Importin-7 mediates memory consolidation through regulation of nuclear translocation of training-activated MAPK in Drosophila.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  9. Review
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

2 authors at 1 institution in 1 country.

Amanda Hicks NatalizioCurriculum in Genetics and Molecular Biology, University of North Carolina, Chapel Hill, NC 27599 Departments of Biology, University of North Carolina, Chapel Hill, NC 27599 Departments of Genetics, University of North Carolina, Chapel Hill, NC 27599 Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, NC 27599 Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, NC 27599.
A Gregory Matera
University of North Carolina at Chapel Hill · US

Funding

ORGANIZATION OF RIBONUCLEOPROTEINS IN MAMMALIAN CELLSR01GM053034 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MATERA, A. GREGORY · 1996 to 2015
$4.3M
NIGMS NIH HHS R01 GM053034NIGMS NIH HHS R01-GM053034
6 · The paper itself

Abstract

Nuclear import is an essential step in small nuclear ribonucleoprotein (snRNP) biogenesis. Snurportin1 (SPN1), the import adaptor, binds to trimethylguanosine (TMG) caps on spliceosomal small nuclear RNAs. Previous studies indicated that vertebrate snRNP import requires importin-β, the transport receptor that binds directly to SPN1. We identify CG42303/snup as the Drosophila orthologue of human snurportin1 (SNUPN). Of interest, the importin-β binding (IBB) domain of SPN1, which is essential for TMG cap-mediated snRNP import in humans, is not well conserved in flies. Consistent with its lack of an IBB domain, we find that Drosophila SNUP (dSNUP) does not interact with Ketel/importin-β. Fruit fly snRNPs also fail to bind Ketel; however, the importin-7 orthologue Moleskin (Msk) physically associates with both dSNUP and spliceosomal snRNPs and localizes to nuclear Cajal bodies. Strikingly, we find that msk-null mutants are depleted of the snRNP assembly factor, survival motor neuron, and the Cajal body marker, coilin. Consistent with a loss of snRNP import function, long-lived msk larvae show an accumulation of TMG cap signal in the cytoplasm. These data indicate that Ketel/importin-β does not play a significant role in Drosophila snRNP import and demonstrate a crucial function for Msk in snRNP biogenesis.

Indexed as

Amino Acid SequenceAnimalsbeta KaryopherinsCell NucleusDrosophila melanogasterDrosophila ProteinsGuanosineHumansKaryopherinsMalpighian TubulesModels, BiologicalMolecular Sequence DataMutationProtein BindingProtein TransportReceptors, Cytoplasmic and Nuclearbeta KaryopherinsDrosophila ProteinsFs(2)Ket protein, DrosophilaGuanosineKaryopherinsMsk protein, DrosophilaN(2),N(2),7-trimethylguanosineReceptors, Cytoplasmic and NuclearRibonucleoproteins, Small NuclearRNA Cap-Binding ProteinsSNUP protein, Drosophila

Identifiers

PMID23885126
PMCPMC3771954
OpenAlexW2085596796

What OpenQuestion holds

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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.