Evidence map›Paper›PMID 27733427›Full record

ArticleThe EMBO journal2016

Chm7 and Heh1 collaborate to link nuclear pore complex quality control with nuclear envelope sealing.

Brant M Webster, David J Thaller, Jens Jäger, Sarah E Ochmann, Sapan Borah, C Patrick Lusk

Abstract read
In one paragraph

Article in The EMBO journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
8.0field-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

92 citing papers in PubMed, 143 citations in OpenAlex.

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  19. International journal of molecular sciences · 2023
    Review
  20. Article

32 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 1 institution in 1 country.

Brant M WebsterDepartment of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
David J ThallerDepartment of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Jens JägerDepartment of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Sarah E OchmannDepartment of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Sapan BorahDepartment of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
C Patrick LuskDepartment of Cell Biology, Yale School of Medicine, New Haven, CT, USA patrick.lusk@yale.edu.ORCID 0000-0003-4703-0533
Yale University · US

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
NIGMS NIH HHS R01 GM105672NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

The integrity of the nuclear envelope barrier relies on membrane remodeling by the ESCRTs, which seal nuclear envelope holes and contribute to the quality control of nuclear pore complexes (NPCs); whether these processes are mechanistically related remains poorly defined. Here, we show that the ESCRT-II/III chimera, Chm7, is recruited to a nuclear envelope subdomain that expands upon inhibition of NPC assembly and is required for the formation of the storage of improperly assembled NPCs (SINC) compartment. Recruitment to sites of NPC assembly is mediated by its ESCRT-II domain and the LAP2-emerin-MAN1 (LEM) family of integral inner nuclear membrane proteins, Heh1 and Heh2. We establish direct binding between Heh2 and the "open" forms of both Chm7 and the ESCRT-III, Snf7, and between Chm7 and Snf7. Interestingly, Chm7 is required for the viability of yeast strains where double membrane seals have been observed over defective NPCs; deletion of CHM7 in these strains leads to a loss of nuclear compartmentalization suggesting that the sealing of defective NPCs and nuclear envelope ruptures could proceed through similar mechanisms.

Indexed as

Adaptor Proteins, Signal TransducingMembrane ProteinsNuclear EnvelopeNuclear PoreNuclear ProteinsProtein BindingProtein MultimerizationSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingChm7 protein, S cerevisiaeMembrane ProteinsNuclear ProteinsSaccharomyces cerevisiae ProteinsSrc1 protein, S cerevisiaeESCRTLEM domainnuclear envelopenuclear transportquality control

Identifiers

PMID27733427
PMCPMC5109239
OpenAlexW2530118867

What OpenQuestion holds

Textmetadata
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.