Evidence map›Paper›PMID 30942170›Full record

ArticleeLife2019

An ESCRT-LEM protein surveillance system is poised to directly monitor the nuclear envelope and nuclear transport system.

David J Thaller, Matteo Allegretti, Sapan Borah, Paolo Ronchi, Martin Beck, C Patrick Lusk

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

82 citing papers in PubMed, 121 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
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  20. Micronuclear collapse from oxidative damage.Science (New York, N.Y.) · 2024
    Article

22 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 2 countries.

David J ThallerDepartment of Cell Biology, Yale School of Medicine, New Haven, United States.ORCID 0000-0003-3577-5562
Matteo AllegrettiStructural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse, Germany.
Sapan BorahDepartment of Cell Biology, Yale School of Medicine, New Haven, United States.
Paolo RonchiElectron Microscopy Core Facility, European Molecular Biology Laboratory, Meyerhofstrasse, Germany.
Martin BeckStructural and Computational Biology Unit, European Molecular Biology Laboratory, Meyerhofstrasse, Germany.ORCID 0000-0002-7397-1321
C Patrick LuskDepartment of Cell Biology, Yale School of Medicine, New Haven, United States.ORCID 0000-0003-4703-0533
Yale University · USEuropean Molecular Biology Laboratory · DEEuropean Molecular Biology Laboratory · DE

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
The mechanism of ESCRT-mediated surveillance of the nuclear envelope barrierR01GM105672 · NIGMS · YALE UNIVERSITY · PI LUSK, CHARLES PATRICK · 2013 to 2025
$4.6M
European Molecular Biology Organization Fellowship 6885European Molecular Biology Organization Fellowship ALTF-1389-2016NIGMS NIH HHS R01 GM105672NIGMS NIH HHS T32 GM007223NIH HHS 5T32GM007223NIH HHS GM105672
6 · The paper itself

Abstract

The integrity of the nuclear membranes coupled to the selective barrier of nuclear pore complexes (NPCs) are essential for the segregation of nucleoplasm and cytoplasm. Mechanical membrane disruption or perturbation to NPC assembly triggers an ESCRT-dependent surveillance system that seals nuclear pores: how these pores are sensed and sealed is ill defined. Using a budding yeast model, we show that the ESCRT Chm7 and the integral inner nuclear membrane (INM) protein Heh1 are spatially segregated by nuclear transport, with Chm7 being actively exported by Xpo1/Crm1. Thus, the exposure of the INM triggers surveillance with Heh1 locally activating Chm7. Sites of Chm7 hyperactivation show fenestrated sheets at the INM and potential membrane delivery at sites of nuclear envelope herniation. Our data suggest that perturbation to the nuclear envelope barrier would lead to local nuclear membrane remodeling to promote membrane sealing. Our findings have implications for disease mechanisms linked to NPC assembly and nuclear envelope integrity.

Indexed as

Active Transport, Cell NucleusAdaptor Proteins, Signal TransducingExportin 1 ProteinKaryopherinsMembrane ProteinsMembrane Transport ProteinsNuclear EnvelopeNuclear PoreReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingChm7 protein, S cerevisiaeExportin 1 ProteinKaryopherinsMembrane ProteinsMembrane Transport ProteinsReceptors, Cytoplasmic and NuclearSaccharomyces cerevisiae ProteinsSrc1 protein, S cerevisiaecell biologyCHMP7ESCRTherniationLEM2nuclear transportS. cerevisiaesurveillance

Identifiers

PMID30942170
PMCPMC6461442
OpenAlexW2929314069

What OpenQuestion holds

Textmetadata
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.