Evidence map›Paper›PMID 28659328›Full record

ArticleThe Journal of cell biology2017

Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.

Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, Elmar Schiebel

Abstract read
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-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

20 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
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  9. Article
  10. A mutation in budding yeastmicroPublication biology · 2021
    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

7 authors at 2 institutions in 1 country.

Diana RüthnickZentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany.ORCID 0000-0001-6365-4050
Annett NeunerZentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany.
Franziska DietrichZentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany.
Daniel KirrmaierZentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany.
Ulrike EngelNikon Imaging Center at the University of Heidelberg, Bioquant, Heidelberg, Germany.
Michael KnopZentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany.
Elmar SchiebelZentrum für Molekulare Biologie at the University of Heidelberg, German Cancer Research Center-Center for Molecular Biology Alliance, Heidelberg, Germany e.schiebel@zmbh.uni-heidelbeg.de.ORCID 0000-0002-3683-247X
German Cancer Research Center · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures. Binding of the γ-tubulin receptor Spc110 to the central plaque from within the nucleus is important for NE insertion of the new SPB. Moreover, we provide evidence that a nuclear pore complex associates with the duplicating SPB and helps to insert the SPB into the NE. After SPB insertion, membrane-associated proteins including the conserved Ndc1 encircle the SPB and retain it within the NE. Thus, uncoupling SPB growth from NE insertion unmasks functions of the duplication machinery.

Indexed as

Cell CycleCalmodulin-Binding ProteinsCytoskeletal ProteinsGenotypeMicroscopy, Electron, TransmissionMicroscopy, FluorescenceMicrotubule-Associated ProteinsMutationNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsPhenotypePhosphoproteinsProtein TransportSaccharomyces cerevisiaeCalmodulin-Binding ProteinsCytoskeletal ProteinsMicrotubule-Associated ProteinsNDC1 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsPhosphoproteinsSaccharomyces cerevisiae ProteinsSPC110 protein, S cerevisiaeSpc29 protein, S cerevisiaeSPC42 protein, S cerevisiaeTubulin

Identifiers

PMID28659328
PMCPMC5551709
OpenAlexW2731672032

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.