Evidence map›Paper›PMID 9151662›Full record

ArticleThe Journal of cell biology1997

Subnuclear trafficking of glucocorticoid receptors in vitro: chromatin recycling and nuclear export.

J Yang, J Liu, D B DeFranco

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. 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
4.3field-weighted citation impact, top 5% 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, 104 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Complex dynamics of transcription regulation.Biochimica et biophysica acta · 2012
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Molecular chaperones function as steroid receptor nuclear mobility factors.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  15. Article
  16. Article
  17. Reconstitution of HIV-1 rev nuclear export: independent requirements for nuclear import and export.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  18. Article
  19. Review
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 1 institution in 1 country.

J YangDepartment of Biological Sciences, University of Pittsburgh, Pennsylvania 15260, USA.
J Liu
D B DeFranco
University of Pittsburgh · US

Funding

INTRACELLULAR MECHANISMS OF GLUCOCORTICOID ACTIONR01CA043037 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI DEFRANCO, DONALD BENEDICT · 1986 to 2005
$1.3M
NCI NIH HHS CA43037NCI NIH HHS R01 CA043037
6 · The paper itself

Abstract

We have used digitonin-permeabilized cells to examine in vitro nuclear export of glucocorticoid receptors (GRs). In situ biochemical extractions in this system revealed a distinct subnuclear compartment, which collects GRs that have been released from chromatin and serves as a nuclear export staging area. Unliganded nuclear GRs within this compartment are not restricted in their subnuclear trafficking as they have the capacity to recycle to chromatin upon rebinding hormone. Thus, GRs that release from chromatin do not require transit through the cytoplasm to regain functionality. In addition, chromatin-released receptors export from nuclei of permeabilized cells in an ATP- and cytosol-independent process that is stimulated by sodium molybdate, other group VI-A transition metal oxyanions, and some tyrosine phosphatase inhibitors. The stimulation of in vitro nuclear export by these compounds is not unique to GR, but is restricted to other proteins such as the 70- and 90-kD heat shock proteins, hsp70 and hsp90, respectively, and heterogeneous nuclear RNP (hnRNP) A1. Under analogous conditions, the 56-kD heat shock protein, hsp56, and hnRNP C do not export from nuclei of permeabilized cells. If tyrosine kinase inhibitors genistein and tyrphostin AG126 are included to prevent increased tyrosine phosphorylation, in vitro nuclear export of GR is inhibited. Thus, our results are consistent with the involvement of a phosphotyrosine system in the general regulation of nuclear protein export, even for proteins such as GR and hnRNP A1 that use distinct nuclear export pathways.

Indexed as

Adenosine TriphosphateAnimalsBiological TransportCell CompartmentationCell Membrane PermeabilityCell NucleusChromatinCorticosteroneDigitoninEnzyme InhibitorsGenisteinHeparinHSP90 Heat-Shock ProteinsIsoflavonesLiverLiver Neoplasms, ExperimentalAdenosine TriphosphateChromatinCorticosteroneDigitoninEnzyme InhibitorsGenisteinHeparinHSP90 Heat-Shock ProteinsIsoflavonesmicrocystinMicrocystinsmolybdateMolybdenumPeptides, CyclicPhosphotyrosineProtein-Tyrosine KinasesProtein Tyrosine PhosphatasesReceptors, GlucocorticoidtungstateTungsten CompoundsVanadates

Identifiers

PMID9151662
PMCPMC2139874
OpenAlexW2125099281

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.