Evidence map›Paper›PMID 18779370›Full record

ArticleThe Journal of cell biology2008

Reshaping of the endoplasmic reticulum limits the rate for nuclear envelope formation.

Daniel J Anderson, Martin W Hetzer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
7.6field-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

124 citing papers in PubMed, 206 citations in OpenAlex.

  1. Inhibition of TFG function causes hereditary axon degeneration by impairing endoplasmic reticulum structure.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Trial
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  7. Confinement-sensitive volume regulation dynamics via high-speed nuclear morphological measurements.Proceedings of the National Academy of Sciences of the United States of America · 2024
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  17. Regulation of organelle size and organization during development.Seminars in cell & developmental biology · 2023
    Review
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  19. Article
  20. Article

64 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

2 authors at 1 institution in 1 country.

Daniel J AndersonMolecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
Martin W Hetzer
Salk Institute for Biological Studies · US

Funding

Nuclear Membrane Fusion in Xenopus Egg ExtractsR01GM073994 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI HETZER, MARTIN W · 2006 to 2010
$1.8M
NIGMS NIH HHS R01 GM073994
6 · The paper itself

Abstract

During mitosis in metazoans, segregated chromosomes become enclosed by the nuclear envelope (NE), a double membrane that is continuous with the endoplasmic reticulum (ER). Recent in vitro data suggest that NE formation occurs by chromatin-mediated reorganization of the tubular ER; however, the basic principles of such a membrane-reshaping process remain uncharacterized. Here, we present a quantitative analysis of nuclear membrane assembly in mammalian cells using time-lapse microscopy. From the initial recruitment of ER tubules to chromatin, the formation of a membrane-enclosed, transport-competent nucleus occurs within approximately 12 min. Overexpression of the ER tubule-forming proteins reticulon 3, reticulon 4, and DP1 inhibits NE formation and nuclear expansion, whereas their knockdown accelerates nuclear assembly. This suggests that the transition from membrane tubules to sheets is rate-limiting for nuclear assembly. Our results provide evidence that ER-shaping proteins are directly involved in the reconstruction of the nuclear compartment and that morphological restructuring of the ER is the principal mechanism of NE formation in vivo.

Indexed as

Carrier ProteinsCell Line, TumorChromatinEndoplasmic ReticulumGreen Fluorescent ProteinsHumansKineticsMembrane ProteinsMyelin ProteinsNerve Tissue ProteinsNogo ProteinsNuclear EnvelopeRecombinant Fusion ProteinsTranscription Factor DP1Carrier ProteinsChromatinGreen Fluorescent ProteinsMembrane ProteinsMyelin ProteinsNerve Tissue ProteinsNogo ProteinsRecombinant Fusion ProteinsRTN3 protein, humanRTN4 protein, humanTranscription Factor DP1

Identifiers

PMID18779370
PMCPMC2528577
OpenAlexW2026862467

What OpenQuestion holds

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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 OpenQuestion graph.