Evidence map›Paper›PMID 28679534›Full record

ArticleThe Journal of biological chemistry2017

Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions.

Aparna Kishor, Elizabeth J F White, Aerielle E Matsangos, Zisui Yan, Bishal Tandukar, Gerald M Wilson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

20 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
  2. Recent insights into HSP70: proteostasis and beyond.Frontiers in molecular biosciences · 2026
    Review
  3. Article
  4. Article
  5. Enhanced HSP70 binding to mBMC plant biology · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Characterization of the interactome profiling ofFrontiers in microbiology · 2022
    Article
  13. Article
  14. Article
  15. Heat shock proteins-driven stress granule dynamics: yet another avenue for cell survival.Apoptosis : an international journal on programmed cell death · 2021
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Review
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

6 authors at 2 institutions in 1 country.

Aparna KishorFrom the Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Elizabeth J F WhiteFrom the Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Aerielle E MatsangosFrom the Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Zisui YanFrom the Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Bishal TandukarFrom the Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201.
Gerald M WilsonFrom the Department of Biochemistry and Molecular Biology and Marlene and Stewart Greenebaum Comprehensive Cancer Center, University of Maryland School of Medicine, Baltimore, Maryland 21201. Electronic address: gwilson@som.umaryland.edu.
University of Maryland, Baltimore · USUniversity of Maryland Marlene and Stewart Greenebaum Comprehensive Cancer Center

Funding

The Nathan Schnaper Intern Program in Translational Cancer ResearchR25CA186872 · NCI · UNIVERSITY OF MARYLAND BALTIMORE · PI BRET A HASSEL, Ian Robert Kleckner · 2015 to 2026
$3.0M
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 CA102428NCI NIH HHS R25 CA186872
6 · The paper itself

Abstract

Hsp70 is a protein chaperone that prevents protein aggregation and aids protein folding by binding to hydrophobic peptide domains through a reversible mechanism directed by an ATPase cycle. However, Hsp70 also binds U-rich RNA including some AU-rich elements (AREs) that regulate the decay kinetics of select mRNAs and has recently been shown to bind and stabilize some ARE-containing transcripts in cells. Previous studies indicated that both the ATP- and peptide-binding domains of Hsp70 contributed to the stability of Hsp70-RNA complexes and that ATP might inhibit RNA recruitment. This suggested the possibility that RNA binding by Hsp70 might mimic features of its peptide-directed chaperone activities. Here, using purified, cofactor-free preparations of recombinant human Hsp70 and quantitative biochemical approaches, we found that high-affinity RNA binding requires at least 30 nucleotides of RNA sequence but is independent of Hsp70's nucleotide-bound status, ATPase activity, or peptide-binding roles. Furthermore, although both the ATP- and peptide-binding domains of Hsp70 could form complexes with an ARE sequence from

Indexed as

Allosteric RegulationAU Rich ElementsBinding SitesHeLa CellsHSP70 Heat-Shock ProteinsHumansImmunoprecipitationKineticsMutationOligopeptidesPeptide FragmentsProtein Interaction Domains and MotifsRecombinant Fusion ProteinsRecombinant ProteinsRibonucleoproteinsRNAFLAG peptideHSP70 Heat-Shock ProteinsHSPA1A protein, humanOligopeptidesPeptide FragmentsRecombinant Fusion ProteinsRecombinant ProteinsRibonucleoproteinsRNARNA, MessengerRNA, recombinantVascular Endothelial Growth Factor AVEGFA protein, humanATPasechaperoneheat shock protein (HSP)mRNA decayRNA-binding protein

Identifiers

PMID28679534
PMCPMC5572911
OpenAlexW2734183401

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.