Evidence map›Paper›PMID 17785525›Full record

ArticleGenes & development2007

HDAC6 controls major cell response pathways to cytotoxic accumulation of protein aggregates.

Cyril Boyault, Yu Zhang, Sabrina Fritah, Cécile Caron, Benoit Gilquin, So Hee Kwon, Carmen Garrido, Tso-Pang Yao, Claire Vourc'h, Patrick Matthias and 1 more

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 180 papers.

0numbers the graph read from it
0cells of the map it votes in
180citing 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

180 citing papers in PubMed, 360 citations in OpenAlex.

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  20. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review

120 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

11 authors at 4 institutions in 3 countries.

Cyril BoyaultInstitut National de la Santé et de la Recherche Médicale (INSERM), U823, Institut Albert Bonniot, Grenoble F-38706, France.
Yu Zhang
Sabrina Fritah
Cécile Caron
Benoit Gilquin
So Hee Kwon
Carmen Garrido
Tso-Pang Yao
Claire Vourc'h
Patrick Matthias
Saadi Khochbin
Institut pour l'avancée des biosciences · FRInserm · FRNovartis (Switzerland) · CHDuke University · US

Funding

Histone deacetylase 6 and aggresome-associated neurodegenerationR01NS054022 · NINDS · DUKE UNIVERSITY · PI YAO, TSO-PANG · 2006 to 2014
$3.1M
NINDS NIH HHS R01 NS054022
6 · The paper itself

Abstract

A cellular defense mechanism counteracts the deleterious effects of misfolded protein accumulation by eliciting a stress response. The cytoplasmic deacetylase HDAC6 (histone deacetylase 6) was previously shown to be a key element in this response by coordinating the clearance of protein aggregates through aggresome formation and their autophagic degradation. Here, for the first time, we demonstrate that HDAC6 is involved in another crucial cell response to the accumulation of ubiquitinated protein aggregates, and unravel its molecular basis. Indeed, our data show that HDAC6 senses ubiquitinated cellular aggregates and consequently induces the expression of major cellular chaperones by triggering the dissociation of a repressive HDAC6/HSF1 (heat-shock factor 1)/HSP90 (heat-shock protein 90) complex and a subsequent HSF1 activation. HDAC6 therefore appears as a master regulator of the cell protective response to cytotoxic protein aggregate formation.

Indexed as

3T3 CellsAcetylationAdenosine TriphosphatasesAnimalsCell Cycle ProteinsDNA-Binding ProteinsHeat-Shock ResponseHeat Shock Transcription FactorsHistone Deacetylase 6Histone DeacetylasesHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLeupeptinsMiceMolecular ChaperonesNuclear ProteinsAdenosine Triphosphatasesbenzyloxycarbonylleucyl-leucyl-leucine aldehydeCell Cycle ProteinsDNA-Binding ProteinsHdac6 protein, mouseHeat Shock Transcription FactorsHistone Deacetylase 6Histone DeacetylasesHsf1 protein, mouseHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsLeupeptinsMolecular ChaperonesNuclear Proteinsp97 ATPaseTranscription FactorsTubulinUbiquitinValosin Containing Protein

Identifiers

PMID17785525
PMCPMC1950856
OpenAlexW1970658265

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.