Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of cell biology - 1 Jun 1996

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

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Cell Division

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cell Line

Share to Cricetinae

Share to Escherichia coli

Share to Gene Expression

Share to Molecular Sequence Data

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 8655589
DOI: 10.1083/jcb.133.5.985
PMCID: PMC2120855

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence using a green fluorescent protein-glucocorticoid receptor chimera that the Ran/TC4 GTPase mediates an essential function independent of nuclear protein import.PMID 8655589Read ↗

Glucocorticoid receptor mutants demonstrate increased motility inside the nucleus of living cells: time of fluorescence recovery after photobleaching (FRAP) is an integrated measure of receptor function.Semantic proximity Read ↗

The C terminus of the nuclear RAN/TC4 GTPase stabilizes the GDP-bound state and mediates interactions with RCC1, RAN-GAP, and HTF9A/RANBP1.Semantic proximity Read ↗

Suppression of cellular transformation by glucocorticoid receptor mutants.Semantic proximity Read ↗

Pathologic human GR mutant has a transdominant negative effect on the wild-type GR by inhibiting its translocation into the nucleus: importance of the ligand-binding domain for intracellular GR trafficking.Semantic proximity Read ↗

Ligand-selective targeting of the glucocorticoid receptor to nuclear subdomains is associated with decreased receptor mobility.Semantic proximity Read ↗

Glucocorticoid receptor dimerization in the cytoplasm might be essential for nuclear localization.Semantic proximity Read ↗

Respiratory Syncytial Virus Nonstructural Protein 1 Blocks Glucocorticoid Receptor Nuclear Translocation by Targeting IPO13 and May Account for Glucocorticoid InsensitivitySemantic proximity Read ↗

Double labelling of subcellular structures with organelle-targeted GFP mutants in vivo.Semantic proximity Read ↗

RanGAP1 induces GTPase activity of nuclear Ras-related Ran.Semantic proximity Read ↗

Statin-induced blockade of prenylation alters nucleocytoplasmic shuttling of GTP-binding proteins gamma2 and beta2 and enhances their suppressive effect on glucocorticoid receptor transcriptional activity.Semantic proximity Read ↗

Nuclear export of glucocorticoid receptor is enhanced by c-Jun N-terminal kinase-mediated phosphorylation.Semantic proximity Read ↗

Rna1p, a Ran/TC4 GTPase activating protein, is required for nuclear import.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.