Evidence map›Paper›PMID 23109422›Full record

ArticleMolecular and cellular biology2013

Hsp70 is a novel posttranscriptional regulator of gene expression that binds and stabilizes selected mRNAs containing AU-rich elements.

Aparna Kishor, Bishal Tandukar, Yann V Ly, Eric A Toth, Yvelisse Suarez, Gary Brewer, Gerald M Wilson

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 65 citations in OpenAlex.

  1. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. A Workflow Guide to RNA-Seq Analysis of Chaperone Function and Beyond.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Heat Stress Tolerance GeneFrontiers in microbiology · 2021
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. A Workflow Guide to RNA-seq Analysis of Chaperone Function and Beyond.Methods in molecular biology (Clifton, N.J.) · 2018
    Article
  20. Article
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

7 authors at 2 institutions in 1 country.

Aparna KishorDepartment of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, Maryland, USA.
Bishal Tandukar
Yann V Ly
Eric A Toth
Yvelisse Suarez
Gary Brewer
Gerald M Wilson
University of Maryland, Baltimore · USUniversity of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

POST TRANSCRIPTIONAL REGULATION--ONCOGENE MESSENGER RNAR01CA052443 · NCI · WAKE FOREST UNIVERSITY · PI BREWER, GARY A. · 1990 to 2012
$4.3M
Mechanisms directing oncoprotein and cytokine mRNA decayR01CA102428 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI WILSON, GERALD M. · 2003 to 2013
$2.8M
NCI NIH HHS R01 CA052443NCI NIH HHS R01 CA102428NCI NIH HHS R01 CA52443
6 · The paper itself

Abstract

The AU-rich elements (AREs) encoded within many mRNA 3' untranslated regions (3'UTRs) are targets for factors that control transcript longevity and translational efficiency. Hsp70, best known as a protein chaperone with well-defined peptide-refolding properties, is known to interact with ARE-like RNA substrates in vitro. Here, we show that cofactor-free preparations of Hsp70 form direct, high-affinity complexes with ARE substrates based on specific recognition of U-rich sequences by both the ATP- and peptide-binding domains. Suppressing Hsp70 in HeLa cells destabilized an ARE reporter mRNA, indicating a novel ARE-directed mRNA-stabilizing role for this protein. Hsp70 also bound and stabilized endogenous ARE-containing mRNAs encoding vascular endothelial growth factor (VEGF) and Cox-2, which involved a mechanism that was unaffected by an inhibitor of its protein chaperone function. Hsp70 recognition and stabilization of VEGF mRNA was mediated by an ARE-like sequence in the proximal 3'UTR. Finally, stabilization of VEGF mRNA coincided with the accumulation of Hsp70 protein in HL60 promyelocytic leukemia cells recovering from acute thermal stress. We propose that the binding and stabilization of selected ARE-containing mRNAs may contribute to the cytoprotective effects of Hsp70 following cellular stress but may also provide a novel mechanism linking constitutively elevated Hsp70 expression to the development of aggressive neoplastic phenotypes.

Indexed as

AU Rich Elements3' Untranslated RegionsBinding SitesCyclooxygenase 2Gene Expression RegulationHeLa CellsHL-60 CellsHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesProtein Structure, TertiaryRNA, MessengerRNA Processing, Post-TranscriptionalRNA StabilityVascular Endothelial Growth Factor A3' Untranslated RegionsCyclooxygenase 2HSP70 Heat-Shock ProteinsMolecular ChaperonesPTGS2 protein, humanRNA, MessengerVascular Endothelial Growth Factor AVEGFA protein, human

Identifiers

PMID23109422
PMCPMC3536313
OpenAlexW2157843092

What OpenQuestion holds

Textmetadata
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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.