Evidence map›Paper›PMID 33464310›Full record

ArticleThe Journal of cell biology2021

Direct binding of ESCRT protein Chm7 to phosphatidic acid-rich membranes at nuclear envelope herniations.

David J Thaller, Danqing Tong, Christopher J Marklew, Nicholas R Ader, Philip J Mannino, Sapan Borah, Megan C King, Barbara Ciani, C Patrick Lusk

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. ESCRT-III function in membrane fission and repair.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. The Inner Nuclear Membrane Has a Unique Lipid Signature.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

David J ThallerDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Danqing TongDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Christopher J MarklewCentre for Chemical Biology, Department of Chemistry, Krebs Institute, University of Sheffield, Brook Hill, Sheffield, UK.
Nicholas R AderDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Philip J ManninoDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Sapan BorahDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Megan C KingDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Barbara CianiCentre for Chemical Biology, Department of Chemistry, Krebs Institute, University of Sheffield, Brook Hill, Sheffield, UK.
C Patrick LuskDepartment of Cell Biology, Yale School of Medicine, New Haven, CT.
Yale University · USUniversity of Sheffield · GB

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
Leveraging cancer-specific defects in nuclear integrity to inform novel synthetic lethal strategiesR21CA231269 · NCI · YALE UNIVERSITY · PI KING, MEGAN C, LUSK, CHARLES PATRICK · 2019 to 2020
$401k
The paradox of 'closed mitosis': using fission yeast to decipher a molecular model of ESCRT activity at the nuclear envelopeF32GM139285 · NIGMS · YALE UNIVERSITY · PI ADER, NICHOLAS RYAN · 2020 to 2022
$201k
NCI NIH HHS R21 CA231269NIGMS NIH HHS F32 GM139285NIGMS NIH HHS R01 GM105672NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Mechanisms that control nuclear membrane remodeling are essential to maintain the integrity of the nucleus but remain to be fully defined. Here, we identify a phosphatidic acid (PA)-binding capacity in the nuclear envelope (NE)-specific ESCRT, Chm7, in budding yeast. Chm7's interaction with PA-rich membranes is mediated through a conserved hydrophobic stretch of amino acids, which confers recruitment to the NE in a manner that is independent of but required for Chm7's interaction with the LAP2-emerin-MAN1 (LEM) domain protein Heh1 (LEM2). Consistent with the functional importance of PA binding, mutation of this region abrogates recruitment of Chm7 to membranes and abolishes Chm7 function in the context of NE herniations that form during defective nuclear pore complex (NPC) biogenesis. In fact, we show that a PA sensor specifically accumulates within these NE herniations. We suggest that local control of PA metabolism is important for ensuring productive NE remodeling and that its dysregulation may contribute to pathologies associated with defective NPC assembly.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceConserved SequenceEndosomal Sorting Complexes Required for TransportHydrophobic and Hydrophilic InteractionsLipid BilayersModels, BiologicalNuclear EnvelopeNuclear PorePhosphatidic AcidsProtein DomainsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingChm7 protein, S cerevisiaeEndosomal Sorting Complexes Required for TransportLipid BilayersPhosphatidic AcidsSaccharomyces cerevisiae Proteins

Identifiers

PMID33464310
PMCPMC7816628
OpenAlexW3122445238

What Socratic 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 Socratic graph.