Evidence map›Paper›PMID 28826471›Full record

ArticleeLife2017

Efficient protein targeting to the inner nuclear membrane requires Atlastin-dependent maintenance of ER topology.

Sumit Pawar, Rosemarie Ungricht, Peter Tiefenboeck, Jean-Christophe Leroux, Ulrike Kutay

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

19 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Transgenic overexpression of bmo-miR-6498-5p increases resistance toApplied and environmental microbiology · 2024
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. A role for endoplasmic reticulum dynamics in the cellular distribution of microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  9. Article
  10. The Diverse Cellular Functions of Inner Nuclear Membrane Proteins.Cold Spring Harbor perspectives in biology · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Atlastin-mediated membrane tethering is critical for cargo mobility and exit from the endoplasmic reticulum.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Article
  18. Article
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Sumit PawarDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.ORCID https://orcid.org/0000-0003-3161-7524
Rosemarie UngrichtDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.
Peter TiefenboeckDepartment of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, ETH Zurich, Zurich, Switzerland.
Jean-Christophe LerouxDepartment of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences, ETH Zurich, Zurich, Switzerland.
Ulrike KutayDepartment of Biology, Institute of Biochemistry, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-8257-7465
ETH Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Newly synthesized membrane proteins are targeted to the inner nuclear membrane (INM) by diffusion within the membrane system of the endoplasmic reticulum (ER), translocation through nuclear pore complexes (NPCs) and retention on nuclear partners. Using a visual in vitro assay we previously showed that efficient protein targeting to the INM depends on nucleotide hydrolysis. We now reveal that INM targeting is GTP-dependent. Exploiting in vitro reconstitution and in vivo analysis of INM targeting, we establish that Atlastins, membrane-bound GTPases of the ER, sustain the efficient targeting of proteins to the INM by their continued activity in preserving ER topology. When ER topology is altered, the long-range diffusional exchange of proteins in the ER network and targeting efficiency to the INM are diminished. Highlighting the general importance of proper ER topology, we show that Atlastins also influence NPC biogenesis and timely exit of secretory cargo from the ER.

Indexed as

Cell NucleusEndoplasmic ReticulumGTP-Binding ProteinsHeLa CellsHumansMembrane ProteinsNuclear EnvelopeProtein BindingProtein TransportATL1 protein, humanGTP-Binding ProteinsMembrane Proteinsatlastinbiochemistrycell biologyERGTPasehumaninner nuclear membranemembrane proteinnuclear envelope

Identifiers

PMID28826471
PMCPMC5587084
OpenAlexW2747560187

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.