Evidence map›Paper›PMID 19416983›Full record

ArticleThe Journal of biological chemistry2009

A unique cytoplasmic localization of retinoic acid receptor-gamma and its regulations.

Young-Hoon Han, Hu Zhou, Jin-Hee Kim, Ting-dong Yan, Kee-Ho Lee, Hua Wu, Feng Lin, Na Lu, Jie Liu, Jin-zhang Zeng and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

21 citing papers in PubMed, 30 citations in OpenAlex.

  1. Review
  2. Review
  3. The Influences of RARγ on the Behavior of Normal and Cancer Stem Cells.International journal of molecular sciences · 2026
    Review
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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

11 authors at 3 institutions in 3 countries.

Young-Hoon HanBurnham Institute for Medical Research, Cancer Center, La Jolla, California 92037, USA. yhhan@kcch.re.kr
Hu Zhou
Jin-Hee Kim
Ting-dong Yan
Kee-Ho Lee
Hua Wu
Feng Lin
Na Lu
Jie Liu
Jin-zhang Zeng
Xiao-kun Zhang
Sanford Burnham Prebys Medical Discovery Institute · USXiamen University · CNKorea Institute of Radiological and Medical Sciences · KR

Funding

Rexinoid Synergy in Prostate Cancer ApoptosisR01CA107039 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI DAWSON, MARCIA I. · 2005 to 2009
$2.5M
15-Deoxy-D12, 14-PGE, J2 as a ligand of RXRalphaR01CA109345 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI ZHANG, XIAO-KUN · 2004 to 2009
$2.4M
TR3/nur77 in Survival and Death of Cancer CellsR01CA087000 · NCI · BURNHAM INSTITUTE FOR MEDICAL RESEARCH · PI ZHANG, XIAO-KUN · 2001 to 2005
$1.5M
NCI NIH HHS CA107039NCI NIH HHS CA109345NCI NIH HHS CA87000NCI NIH HHS R01 CA087000NCI NIH HHS R01 CA107039NCI NIH HHS R01 CA109345NIGMS NIH HHS GM60544
6 · The paper itself

Abstract

Recent evidence suggests that extranuclear action of retinoid receptors is involved in mediating the pleiotropic effects of retinoids. However, whether they reside in the cytoplasm remains elusive. Here, we showed that retinoic acid receptor-gamma (RARgamma) was cytoplasmic in confluent cells, or when cells were released from serum depletion or treated with growth factors. In studying the regulation of RARgamma subcellular localization, we observed that ectopically overexpressed RARgamma was mainly cytoplasmic irrespective of serum concentration and cell density. The cytoplasmic retention of RARgamma was inhibited by ligand retinoic acid (RA). In addition, coexpression of retinoid X receptor-alpha (RXRalpha) resulted in nuclear localization of RARgamma through their heterodimerization. Mutagenesis studies revealed that a C-terminal fragment of RXRalpha potently prevents RA-induced RARgamma nuclear localization and transcriptional function. Furthermore, our results showed that the cytoplasmic retention of RARgamma was due to the presence of its unique N-terminal A/B domain, which was subject to regulation by p38 MAPK-mediated phosphorylation. Deletion or mutation of the N-terminal A/B domain largely impaired its cytoplasmic localization. Together, our data demonstrate that the subcellular localization of RARgamma is regulated by complex interactions among ligand binding, receptor phosphorylation, and receptor dimerizations.

Indexed as

Active Transport, Cell NucleusBlood ProteinsCell CountCell DivisionCell NucleusCulture MediaCytoplasmDimerizationHeLa CellsHumansIntercellular Signaling Peptides and ProteinsKidneyMutagenesisp38 Mitogen-Activated Protein KinasesPhosphorylationProtein Structure, TertiaryBlood ProteinsCulture MediaIntercellular Signaling Peptides and Proteinsp38 Mitogen-Activated Protein KinasesReceptors, Retinoic AcidRetinoic Acid Receptor gammaRetinoid X Receptor alpha

Identifiers

PMID19416983
PMCPMC2709335
OpenAlexW2049538655

What OpenQuestion holds

Textmetadata
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.