Evidence map›Paper›PMID 10859165›Full record

ArticleGenes & development2000

Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes.

R Cuesta, G Laroia, R J Schneider

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
–field-weighted citation impact
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

95 citing papers in PubMed, 191 citations in OpenAlex.

  1. Article
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  6. Stress-Induced Eukaryotic Translational Regulatory Mechanisms.Journal of clinical and medical sciences · 2024
    Article
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  18. Article
  19. mRNA localization is linked to translation regulation in theDevelopment (Cambridge, England) · 2020
    Article
  20. Review

35 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 2 institutions in 1 country.

R CuestaDepartment of Microbiology, New York University School of Medicine and Kaplan Cancer Center, New York, New York 10016 USA.
G Laroia
R J Schneider
Kaplan (United States) · USNew York University · US

Funding

TRANSLATIONAL REGULATION OF ADENOVIRUS GENE EXPRESSIONR01CA042357 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI SCHNEIDER, ROBERT · 1986 to 2004
$1.6M
NCI NIH HHS CA42357NCI NIH HHS R01 CA042357
6 · The paper itself

Abstract

Inhibition of protein synthesis during heat shock limits accumulation of unfolded proteins that might damage eukaryotic cells. We demonstrate that chaperone Hsp27 is a heat shock-induced inhibitor of cellular protein synthesis. Translation of most mRNAs requires formation of a cap-binding initiation complex known as eIF4F, consisting of factors eIF4E, eIF4A, eIF4E kinase Mnk1, poly(A)-binding protein, and adaptor protein eIF4G. Hsp27 specifically bound eIF4G during heat shock, preventing assembly of the cap-initiation/eIF4F complex and trapping eIF4G in insoluble heat shock granules. eIF4G is a specific target of Hsp27, as eIF4E, eIF4A, Mnk1, poly(A)-binding protein, eIF4B, and eIF3 were not bound by Hsp27 and were not recruited into insoluble complexes. Dissociation of eIF4F was enhanced during heat shock by ectopic overexpression of Hsp25, the murine homolog of human Hsp27. Overexpression of Hsc70, a constitutive homolog of Hsp70, prevented loss of cap-initiation complexes and maintained eIF4G solubility. Purified Hsp27 specifically bound purified eIF4G in vitro, prevented in vitro translation, eliminated eIF4G interaction with protein binding factors, and promoted eIF4G insolubilization. These results therefore demonstrate that Hsp27 is a heat-induced inhibitor of eIF4F-dependent mRNA translation.

Indexed as

Heat-Shock ProteinsHSP70 Heat-Shock ProteinsProtein BiosynthesisAnimalsBlotting, WesternCarrier ProteinsCell Line, TransformedDose-Response Relationship, DrugEukaryotic Initiation Factor-4FEukaryotic Initiation Factor-4GFluorescent Antibody TechniqueGlutathione TransferaseHeLa CellsHot TemperatureHSC70 Heat-Shock ProteinsHSP27 Heat-Shock ProteinsCarrier ProteinsEukaryotic Initiation Factor-4FEukaryotic Initiation Factor-4GGlutathione TransferaseHeat-Shock ProteinsHsbp1 protein, mouseHSC70 Heat-Shock ProteinsHSP27 Heat-Shock ProteinsHSP70 Heat-Shock ProteinsHSPA8 protein, humanHspa8 protein, mouseHSPB1 protein, humanIntracellular Signaling Peptides and ProteinsMKNK1 protein, humanMknk1 protein, mouseMolecular ChaperonesNeoplasm ProteinsPeptide Initiation FactorsPhosphotransferasesProtein Serine-Threonine KinasesRNA CapsRNA, Messenger

Identifiers

PMID10859165
PMCPMC316692
OpenAlexW2157894520

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.