Evidence map›Paper›PMID 26040713›Full record

ArticleNature2015

ESCRT-III controls nuclear envelope reformation.

Yolanda Olmos, Lorna Hodgson, Judith Mantell, Paul Verkade, Jeremy G Carlton

Abstract read
In one paragraph

Article in Nature, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 215 papers.

0numbers the graph read from it
0cells of the map it votes in
215citing 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

215 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
  10. Article
  11. Article
  12. Structure, function and assembly of nuclear pore complexes.Nature reviews. Molecular cell biology · 2026
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Yolanda OlmosDivision of Cancer Studies, Section of Cell Biology and Imaging, King's College London, London SE1 1UL, UK.
Lorna HodgsonSchool of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Judith Mantell1] School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK [2] Wolfson Bioimaging Facility, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Paul Verkade1] School of Biochemistry, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK [2] Wolfson Bioimaging Facility, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK [3] School of Physiology &Pharmacology, University of Bristol, Medical Sciences Building, University Walk, Bristol BS8 1TD, UK.
Jeremy G CarltonDivision of Cancer Studies, Section of Cell Biology and Imaging, King's College London, London SE1 1UL, UK.

Funding

Wellcome Trust 093603
6 · The paper itself

Abstract

During telophase, the nuclear envelope (NE) reforms around daughter nuclei to ensure proper segregation of nuclear and cytoplasmic contents. NE reformation requires the coating of chromatin by membrane derived from the endoplasmic reticulum, and a subsequent annular fusion step to ensure that the formed envelope is sealed. How annular fusion is accomplished is unknown, but it is thought to involve the p97 AAA-ATPase complex and bears a topological equivalence to the membrane fusion event that occurs during the abscission phase of cytokinesis. Here we show that the endosomal sorting complex required for transport-III (ESCRT-III) machinery localizes to sites of annular fusion in the forming NE in human cells, and is necessary for proper post-mitotic nucleo-cytoplasmic compartmentalization. The ESCRT-III component charged multivesicular body protein 2A (CHMP2A) is directed to the forming NE through binding to CHMP4B, and provides an activity essential for NE reformation. Localization also requires the p97 complex member ubiquitin fusion and degradation 1 (UFD1). Our results describe a novel role for the ESCRT machinery in cell division and demonstrate a conservation of the machineries involved in topologically equivalent mitotic membrane remodelling events.

Indexed as

Adaptor Proteins, Vesicular TransportCell LineChromatinEndosomal Sorting Complexes Required for TransportHumansIntracellular Signaling Peptides and ProteinsMembrane FusionMitosisNuclear EnvelopeProteinsProtein TransportTelophaseAdaptor Proteins, Vesicular TransportCHMP2A protein, humanChromatinEndosomal Sorting Complexes Required for TransportIntracellular Signaling Peptides and ProteinsProteinsUFD1 protein, human

Identifiers

PMID26040713
PMCPMC4471131

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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.