Evidence map›Paper›PMID 32271860›Full record

ArticleThe Journal of cell biology2020

Regulated lipid synthesis and LEM2/CHMP7 jointly control nuclear envelope closure.

Lauren Penfield, Raakhee Shankar, Erik Szentgyörgyi, Alyssa Laffitte, Michael Sean Mauro, Anjon Audhya, Thomas Müller-Reichert, Shirin Bahmanyar

Open access · greenAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

46 citing papers in PubMed, 74 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 3 institutions in 2 countries.

Lauren PenfieldDepartment of Molecular, Cellular and Developmental Biology, New Haven, CT.
Raakhee ShankarDepartment of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI.
Erik SzentgyörgyiExperimental Center, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Dresden, Germany.
Alyssa LaffitteDepartment of Molecular, Cellular and Developmental Biology, New Haven, CT.
Michael Sean MauroDepartment of Molecular, Cellular and Developmental Biology, New Haven, CT.
Anjon AudhyaDepartment of Biomolecular Chemistry, University of Wisconsin-Madison School of Medicine and Public Health, Madison, WI.
Thomas Müller-ReichertExperimental Center, Faculty of Medicine Carl Gustav Carus, Technische Universität Dresden, Dresden, Germany.
Shirin BahmanyarDepartment of Molecular, Cellular and Developmental Biology, New Haven, CT.
Yale University · USUniversity Hospital Carl Gustav Carus · DEUniversity of Wisconsin–Madison · US

Funding

Molecular mechanisms that regulate vesicle formation and transportR35GM134865 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Anjon Audhya · 2020 to 2026
$4.8M
Molecular Mechanisms that Regulate Lysosomal Protein TransportR01GM088151 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI AUDHYA, ANJON · 2010 to 2019
$3.0M
NIGMS NIH HHS R01 GM088151NIGMS NIH HHS R35 GM134865
6 · The paper itself

Abstract

The nuclear permeability barrier depends on closure of nuclear envelope (NE) holes. Here, we investigate closure of the NE opening surrounding the meiotic spindle in C. elegans oocytes. ESCRT-III components accumulate at the opening but are not required for nuclear closure on their own. 3D analysis revealed cytoplasmic membranes directly adjacent to NE holes containing meiotic spindle microtubules. We demonstrate that the NE protein phosphatase, CNEP-1/CTDNEP1, controls de novo glycerolipid synthesis through lipin to prevent invasion of excess ER membranes into NE holes and a defective NE permeability barrier. Loss of NE adaptors for ESCRT-III exacerbates ER invasion and nuclear permeability defects in cnep-1 mutants, suggesting that ESCRTs restrict excess ER membranes during NE closure. Restoring glycerolipid synthesis in embryos deleted for CNEP-1 and ESCRT components rescued NE permeability defects. Thus, regulating the production and feeding of ER membranes into NE holes together with ESCRT-mediated remodeling is required for nuclear closure.

Indexed as

AnimalsChromatinEndoplasmic ReticulumEndosomal Sorting Complexes Required for TransportHeLa CellsHumansLipidsMembrane ProteinsMiceMicrotubulesMitosisNuclear EnvelopeNuclear ProteinsOrganic ChemicalsPhosphoprotein PhosphatasesSpindle ApparatusCHMP7 protein, humanChromatinCTDNEP1 protein, humanEndosomal Sorting Complexes Required for TransportLEMD2 protein, humanLipidslipineMembrane ProteinsNuclear ProteinsOrganic ChemicalsPhosphoprotein Phosphatases

Identifiers

PMID32271860
PMCPMC7199858
OpenAlexW3015453952

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.