Evidence map›Paper›PMID 10085285›Full record

ArticleThe Journal of cell biology1999

Proteins connecting the nuclear pore complex with the nuclear interior.

C Strambio-de-Castillia, G Blobel, M P Rout

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed
6.9field-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

125 citing papers in PubMed, 223 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The Molecular Architecture of the Nuclear Basket.bioRxiv : the preprint server for biology · 2024
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Evolution and diversification of the nuclear pore complex.Biochemical Society transactions · 2021
    Review
  20. Article

65 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

3 authors at 2 institutions in 1 country.

C Strambio-de-CastilliaLaboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10021, USA.
G Blobel
M P Rout
Rockefeller University · USHoward Hughes Medical Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While much has been learned in recent years about the movement of soluble transport factors across the nuclear pore complex (NPC), comparatively little is known about intranuclear trafficking. We isolated the previously identified Saccharomyces protein Mlp1p (myosin-like protein) by an assay designed to find nuclear envelope (NE) associated proteins that are not nucleoporins. We localized both Mlp1p and a closely related protein that we termed Mlp2p to filamentous structures stretching from the nucleoplasmic face of the NE into the nucleoplasm, similar to the homologous vertebrate and Drosophila Tpr proteins. Mlp1p can be imported into the nucleus by virtue of a nuclear localization sequence (NLS) within its COOH-terminal domain. Overexpression experiments indicate that Mlp1p can form large structures within the nucleus which exclude chromatin but appear highly permeable to proteins. Remarkably, cells harboring a double deletion of MLP1 and MLP2 were viable, although they showed a slower net rate of active nuclear import and faster passive efflux of a reporter protein. Our data indicate that the Tpr homologues are not merely NPC-associated proteins but that they can be part of NPC-independent, peripheral intranuclear structures. In addition, we suggest that the Tpr filaments could provide chromatin-free conduits or tracks to guide the efficient translocation of macromolecules between the nucleoplasm and the NPC.

Indexed as

Saccharomyces cerevisiae ProteinsAmino Acid SequenceBiological TransportCell NucleusCloning, MolecularFungal ProteinsGene DeletionGreen Fluorescent ProteinsLuminescent ProteinsMicroscopy, ElectronMolecular Sequence DataNuclear EnvelopeNuclear Pore Complex ProteinsNuclear ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsFungal ProteinsGreen Fluorescent ProteinsLuminescent ProteinsMLP1 protein, S cerevisiaeMLP2 protein, S cerevisiaeNuclear Pore Complex ProteinsNuclear ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID10085285
PMCPMC2148185
OpenAlexW1990695832

What OpenQuestion holds

Texttitle and abstract
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.