Evidence map›Paper›PMID 12093788›Full record

ArticleThe Journal of cell biology2002

Interference with the cytoplasmic tail of gp210 disrupts "close apposition" of nuclear membranes and blocks nuclear pore dilation.

Sheona P Drummond, Katherine L Wilson

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

15 citing papers in PubMed, 58 citations in OpenAlex.

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  8. Biology and biophysics of the nuclear pore complex and its components.International review of cell and molecular biology · 2008
    Review
  9. Topology of yeast Ndc1p: predictions for the human NDC1/NET3 homologue.The anatomical record. Part A, Discoveries in molecular, cellular, and evolutionary biology · 2006
    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

2 authors at 2 institutions in 1 country.

Sheona P DrummondDepartment of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Katherine L Wilson
Johns Hopkins Medicine · USJohns Hopkins University · US

Funding

REGULATION OF NUCLEAR ENVELOPE ASSEMBLY AND DISASSEMBLYR01GM048646 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI WILSON, KATHERINE L · 1994 to 2012
$4.9M
NIGMS NIH HHS R01 GM048646NIGMS NIH HHS R01-GM48646Wellcome Trust
6 · The paper itself

Abstract

We tested the hypothesis that gp210, an integral membrane protein of nuclear pore complexes (NPCs), mediates nuclear pore formation. Gp210 has a large lumenal domain and small COOH-terminal tail exposed to the cytoplasm. We studied the exposed tail. We added recombinant tail polypeptides to Xenopus nuclear assembly extracts, or inhibited endogenous gp210 tails using anti-tail antibodies. Both strategies had no effect on the formation of fused flattened nuclear membranes, but blocked NPC assembly and nuclear growth. Inhibited nuclei accumulated gp210 and some nucleoporin p62, but failed to incorporate nup214/CAN, nup153, or nup98 and were defective for nuclear import of lamin B3. Scanning and transmission EM revealed a lack of "closely apposed" inner and outer membranes, and the accumulation of novel arrested structures including "mini-pores." We conclude that gp210 has early roles in nuclear pore formation, and that pore dilation is mediated by gp210 and its tail-binding partner(s). We propose that membrane fusion and pore dilation are coupled, acting as a mechanism to control nuclear pore size.

Indexed as

Amino Acid SequenceAnimalsCell MembraneCell NucleusCytoplasmDNA, ComplementaryDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelGlutathione TransferaseImmunoblottingIntermediate Filament ProteinsLamin Type BMembrane FusionMembrane GlycoproteinsMicroscopy, ElectronMicroscopy, Electron, ScanningDNA, ComplementaryGlutathione TransferaseIntermediate Filament ProteinsLamin Type BMembrane GlycoproteinsNuclear Pore Complex ProteinsNuclear ProteinsNUP210 protein, XenopusRecombinant Fusion ProteinsThrombinXenopus Proteins

Identifiers

PMID12093788
PMCPMC2173024
OpenAlexW2045564536

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.