Evidence map›Paper›PMID 12242302›Full record

ArticleMolecular and cellular biology2002

Highly selective actions of HuR in antagonizing AU-rich element-mediated mRNA destabilization.

Chyi-Ying A Chen, Nianhua Xu, Ann-Bin Shyu

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

100 citing papers in PubMed, 175 citations in OpenAlex.

  1. Article
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  3. Article
  4. Review
  5. Review
  6. Article
  7. Relationship between HuR and tumor drug resistance.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2023
    Review
  8. Article
  9. Review
  10. RNA-Binding Protein HuR Promotes Airway Inflammation in a House Dust Mite-Induced Allergic Asthma Model.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

40 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

3 authors at 1 institution in 1 country.

Chyi-Ying A ChenDepartment of Biochemistry and Molecular Biology, University of Texas Medical School, Houston, Texas 77030, USA.
Nianhua Xu
Ann-Bin Shyu
The University of Texas at Austin · US

Funding

Messenger RNA Turnover in Mammalian CellsR01GM046454 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR HOUSTON · PI SHYU, ANN-BIN · 1991 to 2016
$7.1M
NIGMS NIH HHS GM 46454NIGMS NIH HHS R01 GM046454
6 · The paper itself

Abstract

Human RNA-binding protein HuR, a nucleocytoplasmic shuttling protein, is a ubiquitously expressed member of the family of Hu proteins, which consist of two N-terminal RNA recognition motifs (RRM1 and RRM2), a hinge region, and a C-terminal RRM (RRM3). Although in vitro experiments showed indiscriminate binding of Hu proteins synthesized in bacterial systems to many different AU-rich elements (AREs), in vivo studies have pointed to a cytoplasmic role for HuR protein in antagonizing the rapid decay of some specific ARE-containing mRNAs, depending on physiological situations. By ectopically overexpressing HuR and its mutant derivatives in NIH 3T3 cells to mimic HuR upregulation of specific ARE-containing mRNAs in other systems, we have examined the in vivo ARE-binding specificity of HuR and dissected its functionally critical domains. We show that in NIH 3T3 cells, HuR stabilizes reporter messages containing only the c-fos ARE and not other AREs. Two distinct binding sites were identified within the c-fos ARE, the 5' AUUUA-containing domain and the 3' U-stretch-containing domain. These actions of HuR are markedly different from those of another ARE-binding protein, hnRNP D (also termed AUF1), which in vivo recognizes AUUUA repeats found in cytokine AREs and can exert both stabilizing and destabilizing effects. Further experiments showed that any combination of two of the three RRM domains of HuR is sufficient for strong binding to the c-fos ARE in vitro and to exert an RNA stabilization effect in vivo comparable to that of intact HuR and that the hinge region containing nucleocytoplasmic shuttling signals is dispensable for the stabilization effect of HuR. Our data suggest that the ARE-binding specificity of HuR in vivo is modulated to interact only with and thus regulate specific AREs in a cell type- and physiological state-dependent manner.

Indexed as

Antigens, SurfaceHeterogeneous-Nuclear Ribonucleoprotein DRNA Stability3T3 CellsAnimalsBase SequenceBinding SitesCell NucleusELAV-Like Protein 1ELAV ProteinsHeterogeneous Nuclear Ribonucleoprotein D0Heterogeneous-Nuclear RibonucleoproteinsHumansMiceMolecular Sequence DataProto-Oncogene Proteins c-fosAntigens, SurfaceELAVL1 protein, humanELAV-Like Protein 1ELAV ProteinsHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0Heterogeneous-Nuclear RibonucleoproteinsHNRNPD protein, humanHnrpd protein, mouseProto-Oncogene Proteins c-fosRibonucleoproteinsRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID12242302
PMCPMC139819
OpenAlexW2154122744

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.