Evidence map›Paper›PMID 24165936›Full record

ArticleThe Journal of cell biology2013

The transmission of nuclear pore complexes to daughter cells requires a cytoplasmic pool of Nsp1.

Paolo Colombi, Brant M Webster, Florian Fröhlich, C Patrick Lusk

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In one paragraph

Article in The Journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

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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

4 authors.

Paolo ColombiDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Brant M Webster
Florian Fröhlich
C Patrick Lusk

Funding

The mechanism of ESCRT-mediated surveillance of the nuclear envelope barrierR01GM105672 · NIGMS · YALE UNIVERSITY · PI LUSK, CHARLES PATRICK · 2013 to 2025
$4.6M
NIGMS NIH HHS R01 GM105672NIGMS NIH HHS R01GM105672
6 · The paper itself

Abstract

Nuclear pore complexes (NPCs) are essential protein assemblies that span the nuclear envelope and establish nuclear-cytoplasmic compartmentalization. We have investigated mechanisms that control NPC number in mother and daughter cells during the asymmetric division of budding yeast. By simultaneously tracking existing NPCs and newly synthesized NPC protomers (nups) through anaphase, we uncovered a pool of the central channel nup Nsp1 that is actively targeted to the bud in association with endoplasmic reticulum. Bud targeting required an intact actin cytoskeleton and the class V myosin, Myo2. Selective inhibition of cytoplasmic Nsp1 or inactivation of Myo2 reduced the inheritance of NPCs in daughter cells, leading to a daughter-specific loss of viability. Our data are consistent with a model in which Nsp1 releases a barrier that otherwise prevents NPC passage through the bud neck. It further supports the finding that NPC inheritance, not de novo NPC assembly, is primarily responsible for controlling NPC number in daughter cells.

Indexed as

MitosisActin CytoskeletonAnaphaseCytoplasmEndoplasmic ReticulumHeredityMicrobial ViabilityMicroscopy, FluorescenceMyosin Heavy ChainsMyosin Type VNuclear PoreNuclear Pore Complex ProteinsNuclear ProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsMYO2 protein, S cerevisiaeMyosin Heavy ChainsMyosin Type VNSP1 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID24165936
PMCPMC3812967

What OpenQuestion holds

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Registered trials

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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.