Evidence map›Paper›PMID 19165341›Full record

ArticlePloS one2009

Nuclear envelope remnants: fluid membranes enriched in sterols and polyphosphoinositides.

Marie Garnier-Lhomme, Richard D Byrne, Tina M C Hobday, Stephen Gschmeissner, Rudiger Woscholski, Dominic L Poccia, Erick J Dufourc, Banafshé Larijani

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

17 citing papers in PubMed, 45 citations in OpenAlex.

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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

8 authors at 5 institutions in 3 countries.

Marie Garnier-LhommeCell Biophysics Laboratory, Lincoln's Inn Fields Laboratories, Cancer Research UK, London, United Kingdom.
Richard D Byrne
Tina M C Hobday
Stephen Gschmeissner
Rudiger Woscholski
Dominic L Poccia
Erick J Dufourc
Banafshé Larijani
The Honourable Society of Lincoln's Inn · GBInstitut National Polytechnique de Toulouse · FRAmherst College · USCancer Research UK · GBImperial College London · GB

Funding

Cancer Research UKMedical Research Council G0000138
6 · The paper itself

Abstract

backgroundThe cytoplasm of eukaryotic cells is a highly dynamic compartment where membranes readily undergo fission and fusion to reorganize the cytoplasmic architecture, and to import, export and transport various cargos within the cell. The double membrane of the nuclear envelope that surrounds the nucleus, segregates the chromosomes from cytoplasm and regulates nucleocytoplasmic transport through pores. Many details of its formation are still unclear. At fertilization the sperm devoid of nuclear envelope pores enters the egg. Although most of the sperm nuclear envelope disassembles, remnants of the envelope at the acrosomal and centriolar fossae do not and are subsequently incorporated into the newly forming male pronuclear envelope. Remnants are conserved from annelid to mammalian sperm. METHODOLOGY/PRINCIPAL

findingsUsing lipid mass spectrometry and a new application of deuterium solid-state NMR spectroscopy we have characterized the lipid composition and membrane dynamics of the sperm nuclear envelope remnants in isolated sperm nuclei. CONCLUSIONS/SIGNIFICANCE: We report nuclear envelope remnants are relatively fluid membranes rich in sterols, devoid of sphingomyelin, and highly enriched in polyphosphoinositides and polyunsaturated phospholipids. The localization of the polybasic effector domain of MARCKS illustrates the non-nuclear aspect of the polyphosphoinositides. Based on their atypical biophysical characteristics and phospholipid composition, we suggest a possible role for nuclear envelope remnants in membrane fusion leading to nuclear envelope assembly.

Indexed as

AnimalsCell-Free SystemFemaleFertilizationIntracellular Signaling Peptides and ProteinsLipid BilayersMagnetic Resonance SpectroscopyMaleMembrane ProteinsMicroscopy, Electron, TransmissionModels, BiologicalMyristoylated Alanine-Rich C Kinase SubstrateNuclear EnvelopePhosphatidylinositol PhosphatesSea UrchinsSpermatozoaIntracellular Signaling Peptides and ProteinsLipid BilayersMembrane ProteinsMyristoylated Alanine-Rich C Kinase SubstratePhosphatidylinositol PhosphatesSterols

Identifiers

PMID19165341
PMCPMC2626249
OpenAlexW2069096799

What OpenQuestion holds

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LicenceCC BY
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.