Evidence map›Paper›PMID 8909533›Full record

ArticleThe Journal of cell biology1996

RanBP1 stabilizes the interaction of Ran with p97 nuclear protein import.

N C Chi, E J Adam, G D Visser, S A Adam

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
12.1field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 175 citations in OpenAlex.

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  12. Identification of protein cofactors necessary for sequence-specific plasmid DNA nuclear import.Molecular therapy : the journal of the American Society of Gene Therapy · 2009
    Article
  13. Article
  14. Article
  15. Regulation of nuclear lamin polymerization by importin alpha.The Journal of biological chemistry · 2008
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

13 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

4 authors at 1 institution in 1 country.

N C ChiDepartment of Cell and Molecular Biology, Northwestern University Medical School, Chicago, Illinois 60611, USA.
E J Adam
G D Visser
S A Adam
Northwestern University · US

Funding

MEDICAL SCIENTIST TRAINING PROGRAMT32GM008152 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ARDEHALI, HOSSEIN · 1987 to 2021
$24.0M
CARCINOGENESIS TRAINING PROGRAMT32CA009560 · NCI · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Kathleen Janee Green · 1986 to 2026
$8.4M
CYTOPLASMIC FACTORS IN NUCLEAR PROTEIN IMPORTR01GM047866 · NIGMS · NORTHWESTERN UNIVERSITY · PI ADAM, STEPHEN A · 1992 to 2000
$271k
NCI NIH HHS 5-T32 CA 09560NIGMS NIH HHS 5-T32-GM08152-10NIGMS NIH HHS GM 47866
6 · The paper itself

Abstract

Three factors have been identified that reconstitute nuclear protein import in a permeabilized cell assay: the NLS receptor, p97, and Ran/TC4. Ran/TC4, in turn, interacts with a number of proteins that are involved in the regulation of GTP hydrolysis or are components of the nuclear pore. Two Ran-binding proteins, RanBP1 and RanBP2, form discrete complexes with p97 as demonstrated by immunoadsorption from HeLa cell extracts fractionated by gel filtration chromatography. A > 400-kD complex contains p97, Ran, and RanBP2. Another complex of 150-300 kD was comprised of p97, Ran, and RanBP1. This second trimeric complex could be reconstituted from recombinant proteins. In solution binding assays, Ran-GTP bound p97 with high affinity, but the binding of Ran-GDP to p97 was undetectable. The addition of RanBP1 with Ran-GDP or Ran-GTP increased the affinity of both forms of Ran for p97 to the same level. Binding of Ran-GTP to p97 dissociated p97 from immobilized NLS receptor while the Ran-GDP/RanBP1/p97 complex did not dissociate from the receptor. In a digitonin-permeabilized cell docking assay, RanBP1 stabilizes the receptor complex against temperature-dependent release from the pore. When added to an import assay with recombinant NLS receptor, p97 and Ran-GDP, RanBP1 significantly stimulates transport. These results suggest that RanBP1 promotes both the docking and translocation steps in nuclear protein import by stabilizing the interaction of Ran-GDP with p97.

Indexed as

Nuclear Pore Complex Proteinsalpha Karyopherinsbeta KaryopherinsBiological TransportCell Membrane PermeabilityCell NucleusDigitoninDNA-Binding ProteinsGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateHeLa CellsHumansMacromolecular SubstancesMolecular ChaperonesNuclear Envelopealpha Karyopherinsbeta KaryopherinsDigitoninDNA-Binding ProteinsGTP-Binding ProteinsGuanosine DiphosphateGuanosine TriphosphateMacromolecular SubstancesMolecular ChaperonesNuclear Pore Complex ProteinsNuclear Proteinsran-binding protein 1ran-binding protein 2ran GTP-Binding ProteinRecombinant Fusion Proteins

Identifiers

PMID8909533
PMCPMC2121062
OpenAlexW2147065993

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.