Evidence map›Paper›PMID 27831465›Full record

ArticleeLife2016

Dynamic control of Hsf1 during heat shock by a chaperone switch and phosphorylation.

Xu Zheng, Joanna Krakowiak, Nikit Patel, Ali Beyzavi, Jideofor Ezike, Ahmad S Khalil, David Pincus

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 151 papers.

0numbers the graph read from it
0cells of the map it votes in
151citing papers in PubMed
11.3field-weighted citation impact, top 1% 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

151 citing papers in PubMed, 254 citations in OpenAlex.

  1. Article
  2. Article
  3. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
    Review
  4. Article
  5. The role of the nucleus in the control of mitochondrial precursor proteins in yeast.Protein science : a publication of the Protein Society · 2026
    Review
  6. Article
  7. Quality control of protein import into mammalian mitochondria.Protein science : a publication of the Protein Society · 2026
    Review
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  9. Article
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  11. Review
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  15. Article
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91 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Xu ZhengWhitehead Institute for Biomedical Research, Cambridge, United States.
Joanna KrakowiakWhitehead Institute for Biomedical Research, Cambridge, United States.
Nikit PatelDepartment of Biomedical Engineering and Biological Design Center, Boston University, Boston, United States.
Ali BeyzaviDepartment of Mechanical Engineering, Boston University, Boston, United States.
Jideofor EzikeWhitehead Institute for Biomedical Research, Cambridge, United States.
Ahmad S KhalilDepartment of Biomedical Engineering and Biological Design Center, Boston University, Boston, United States.
David PincusWhitehead Institute for Biomedical Research, Cambridge, United States.ORCID 0000-0002-9651-6858
Whitehead Institute for Biomedical Research · USBoston University · US

Funding

Quantitative approaches to reveal the homeostatic control mechanisms of stress reDP5OD017941 · OD · WHITEHEAD INSTITUTE FOR BIOMEDICAL RES · PI PINCUS, DAVID · 2013 to 2017
$2.4M
NIH HHS DP5 OD017941
6 · The paper itself

Abstract

Heat shock factor (Hsf1) regulates the expression of molecular chaperones to maintain protein homeostasis. Despite its central role in stress resistance, disease and aging, the mechanisms that control Hsf1 activity remain unresolved. Here we show that in budding yeast, Hsf1 basally associates with the chaperone Hsp70 and this association is transiently disrupted by heat shock, providing the first evidence that a chaperone repressor directly regulates Hsf1 activity. We develop and experimentally validate a mathematical model of Hsf1 activation by heat shock in which unfolded proteins compete with Hsf1 for binding to Hsp70. Surprisingly, we find that Hsf1 phosphorylation, previously thought to be required for activation, in fact only positively tunes Hsf1 and does so without affecting Hsp70 binding. Our work reveals two uncoupled forms of regulation - an ON/OFF chaperone switch and a tunable phosphorylation gain - that allow Hsf1 to flexibly integrate signals from the proteostasis network and cell signaling pathways.

Indexed as

Hot TemperatureProtein Processing, Post-TranslationalDNA-Binding ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsModels, TheoreticalPhosphorylationProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsDNA-Binding ProteinsHeat-Shock ProteinsHSF1 protein, S cerevisiaeHSP70 Heat-Shock ProteinsSaccharomyces cerevisiae ProteinsTranscription Factorscell biologychaperonecomputational biologyheat shockHsf1Hsp70phosphorylationS. cerevisiaesystems biologysystems modeling

Identifiers

PMID27831465
PMCPMC5127643
OpenAlexW2551516228

What OpenQuestion holds

Textmetadata
LicenceCC0
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.