Evidence map›Paper›PMID 21444689›Full record

ArticleThe Journal of cell biology2011

System analysis shows distinct mechanisms and common principles of nuclear envelope protein dynamics.

Nikolaj Zuleger, David A Kelly, A Christine Richardson, Alastair R W Kerr, Martin W Goldberg, Andrew B Goryachev, Eric C Schirmer

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
3.7field-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

58 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
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  10. Article
  11. Review
  12. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  13. Proximity proteomics of synaptopodin provides insight into the molecular composition of the spine apparatus of dendritic spines.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021
    Review
  18. Article
  19. Article
  20. Article
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

7 authors at 4 institutions in 2 countries.

Nikolaj ZulegerThe Wellcome Trust Centre for Cell Biology, Scotland, UK.
David A Kelly
A Christine Richardson
Alastair R W Kerr
Martin W Goldberg
Andrew B Goryachev
Eric C Schirmer
Durham University · GBInstitute of Cell Biology · UAUniversity of Edinburgh · GBWellcome Centre for Cell Biology · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E015735/1Wellcome Trust 076616Wellcome Trust 079658Wellcome Trust 095209
6 · The paper itself

Abstract

The nuclear envelope contains >100 transmembrane proteins that continuously exchange with the endoplasmic reticulum and move within the nuclear membranes. To better understand the organization and dynamics of this system, we compared the trafficking of 15 integral nuclear envelope proteins using FRAP. A surprising 30-fold range of mobilities was observed. The dynamic behavior of several of these proteins was also analyzed after depletion of ATP and/or Ran, two functions implicated in endoplasmic reticulum-inner nuclear membrane translocation. This revealed that ATP- and Ran-dependent translocation mechanisms are distinct and not used by all inner nuclear membrane proteins. The Ran-dependent mechanism requires the phenylalanine-glycine (FG)-nucleoporin Nup35, which is consistent with use of the nuclear pore complex peripheral channels. Intriguingly, the addition of FGs to membrane proteins reduces FRAP recovery times, and this also depends on Nup35. Modeling of three proteins that were unaffected by either ATP or Ran depletion indicates that the wide range in mobilities could be explained by differences in binding affinities in the inner nuclear membrane.

Indexed as

Adenosine TriphosphateAnimalsCell NucleusComputational BiologyEndoplasmic ReticulumHeLa CellsHumansMembrane ProteinsMiceMolecular Dynamics SimulationNuclear Enveloperan GTP-Binding ProteinRatsAdenosine TriphosphateMembrane Proteinsran GTP-Binding Protein

Identifiers

PMID21444689
PMCPMC3082195
OpenAlexW2122778614

What OpenQuestion 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 OpenQuestion graph.