Evidence map›Paper›PMID 25303532›Full record

ArticleCell2014

Surveillance of nuclear pore complex assembly by ESCRT-III/Vps4.

Brant M Webster, Paolo Colombi, Jens Jäger, C Patrick Lusk

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 144 papers.

0numbers the graph read from it
0cells of the map it votes in
144citing papers in PubMed
9.4field-weighted citation impact, top 1% 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

144 citing papers in PubMed, 243 citations in OpenAlex.

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  18. Nuclear envelope budding: Getting large macromolecular complexes out of the nucleus.BioEssays : news and reviews in molecular, cellular and developmental biology · 2024
    Article
  19. Article
  20. On the origin of the nucleus: a hypothesis.Microbiology and molecular biology reviews : MMBR · 2023
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Brant M WebsterDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA.
Paolo ColombiDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA.
Jens JägerDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA.
C Patrick LuskDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520, USA. Electronic address: patrick.lusk@yale.edu.
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
Genomic Regulation at the Nuclear PeripheryR21HG006742 · NHGRI · YALE UNIVERSITY · PI KING, MEGAN C, LUSK, CHARLES PATRICK · 2013 to 2014
$458k
NHGRI NIH HHS R21 HG006742NHGRI NIH HHS R21HG006742NIGMS NIH HHS 5T32GM007223NIGMS NIH HHS R01 GM105672NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

The maintenance of nuclear compartmentalization by the nuclear envelope and nuclear pore complexes (NPCs) is essential for cell function; loss of compartmentalization is associated with cancers, laminopathies, and aging. We uncovered a pathway that surveils NPC assembly intermediates to promote the formation of functional NPCs. Surveillance is mediated by Heh2, a member of the LEM (Lap2-emerin-MAN1) family of integral inner nuclear membrane proteins, which binds to an early NPC assembly intermediate, but not to mature NPCs. Heh2 recruits the endosomal sorting complex required for transport (ESCRT)-III subunit Snf7 and the AAA-ATPase Vps4 to destabilize and clear defective NPC assembly intermediates. When surveillance or clearance is compromised, malformed NPCs accumulate in a storage of improperly assembled nuclear pore complexes compartment, or SINC. The SINC is retained in old mothers to prevent loss of daughter lifespan, highlighting a continuum of mechanisms to ensure nuclear compartmentalization.

Indexed as

Active Transport, Cell NucleusAdenosine TriphosphatasesEndosomal Sorting Complexes Required for TransportNuclear PoreSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsAdenosine TriphosphatasesEndosomal Sorting Complexes Required for TransportSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsVPS4 protein, S cerevisiaeVps4 protein, S pombe

Identifiers

PMID25303532
PMCPMC4194032
OpenAlexW2074577396

What OpenQuestion holds

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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.