Evidence map›Paper›PMID 8655589›Full record

ArticleThe Journal of cell biology1996

Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import.

K L Carey, S A Richards, K M Lounsbury, I G Macara

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 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
10.3field-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

48 citing papers in PubMed, 156 citations in OpenAlex.

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  18. Charting biologically relevant chemical space: a structural classification of natural products (SCONP).Proceedings of the National Academy of Sciences of the United States of America · 2005
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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.

K L CareyDepartment of Pathology, University of Vermont, Burlington, 05405-0068, USA.
S A Richards
K M Lounsbury
I G Macara
University of Vermont · US

Funding

The RAN GTPaseR01GM050526 · NIGMS · VANDERBILT UNIVERSITY · PI MACARA, IAN G · 1994 to 2014
$4.8M
ENVIRONMENTAL PATHOLOGY TRAINING PROGRAMT32ES007122 · NIEHS · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI VAN DER VLIET, ALBERT · 1985 to 2012
$4.2M
REGULATION AND INTERACTIONS OF RAN DURING THE CELL CYCLEF32CA063801 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LOUNSBURY, KAREN M · 1994 to 1995
–
NCI NIH HHS F32CA63801NIEHS NIH HHS EST3207122NIGMS NIH HHS GM50526
6 · The paper itself

Abstract

The Ran/TC4 GTPase is required for the nuclear accumulation of artificial karyophiles in permeabilized cell assays. To investigate Ran function in a physiologically intact setting using mammalian cells, we examined the effects of several Ran mutants on cell growth and on the nuclear translocation of a glucocorticoid receptor-green fluorescent protein fusion (GR-GFP). Glucocorticoid receptor is cytosolic in the absence of ligand, but translocates to the nucleus on binding the agonist dexamethasone. After transfection into baby hamster kidney cells (BHK21), GR-GFP was detectable in living cells by direct fluorescence microscopy. Addition of dexamethasone caused a rapid translocation of the chimeric protein from the cytosol into the nucleus (t1/2 approximately 5 min). Cotransfection with epitope-tagged, wild-type Ran led to expression of HA1-Ran that was approximately 1.6-fold higher than the level of the endogenous protein, but it had no deleterious effect on nuclear import of the GR-GFP. However, expression of the Ran mutants G19V, T24N, or a COOH-terminal deletion (delta C) mutant dramatically reduced the accumulation of GR-GFP in the nuclei. An L43E mutant of Ran was without significant effect on nuclear GR-GFP import. Identical results were obtained following micro-injection of recombinant Ran mutants into cells expressing GR-GFP. Significantly, all of the Ran mutants, including L43E, strongly inhibited cell growth. These results demonstrate the use of GR-GFP in real-time imaging of nuclear transport. They also show that multiple types of Ran mutant exert dominant effects on this process, and that normal Ran function requires cycling between the GTP- and GDP-bound states of the protein. Most importantly, the results with the L43E Ran mutant provide strong evidence that Ran mediates a function essential to cell viability that is independent of nuclear protein import.

Indexed as

Amino Acid SequenceAnimalsBiological Transport, ActiveCell DivisionCell LineCell NucleusCricetinaeEscherichia coliGene ExpressionGreen Fluorescent ProteinsGTP PhosphohydrolasesLuminescent ProteinsMicroinjectionsMolecular Sequence DataMutationNuclear ProteinsGreen Fluorescent ProteinsGTP PhosphohydrolasesLuminescent ProteinsNuclear Proteinsran GTP-Binding ProteinReceptors, GlucocorticoidRecombinant Fusion Proteins

Identifiers

PMID8655589
PMCPMC2120855
OpenAlexW2052059014

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.