Evidence map›Paper›PMID 30605679›Full record

ArticleCell reports2019

SUMOylation and the HSF1-Regulated Chaperone Network Converge to Promote Proteostasis in Response to Heat Shock.

Frauke Liebelt, Rebecca M Sebastian, Christopher L Moore, Monique P C Mulder, Huib Ovaa, Matthew D Shoulders, Alfred C O Vertegaal

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

30 citing papers in PubMed, 62 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. HSF1 Activation Mechanisms, Disease Roles, and Small Molecule Therapeutics.International journal of biological sciences · 2025
    Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Signalling mechanisms and cellular functions of SUMO.Nature reviews. Molecular cell biology · 2022
    Review
  18. Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022
    Article
  19. 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 2 countries.

Frauke LiebeltDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2300 RA, the Netherlands.
Rebecca M SebastianDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Christopher L MooreDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Monique P C MulderOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2300 RA, the Netherlands.
Huib OvaaOncode Institute and Department of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2300 RA, the Netherlands.
Matthew D ShouldersDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. Electronic address: mshoulde@mit.edu.
Alfred C O VertegaalDepartment of Cell and Chemical Biology, Leiden University Medical Center, Leiden 2300 RA, the Netherlands. Electronic address: vertegaal@lumc.nl.
Leiden University Medical Center · NLMassachusetts Institute of Technology · US

Funding

TOXICOLOGY CORE UNITP30ES002109 · NIEHS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI YAFFE, MICHAEL B · 1985 to 2020
$25.6M
Aggregate Proximity-Induced, Proteostasis Network-Modulated Destabilization of the ProteomeR21AG054961 · NIA · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SHOULDERS, MATTHEW DONALD · 2016 to 2017
$420k
European Research Council 310913NIA NIH HHS R21 AG054961NIEHS NIH HHS P30 ES002109
6 · The paper itself

Abstract

The role of stress-induced increases in SUMO2/3 conjugation during the heat shock response (HSR) has remained enigmatic. We investigated SUMO signal transduction at the proteomic and functional level during the HSR in cells depleted of proteostasis network components via chronic heat shock factor 1 inhibition. In the recovery phase post heat shock, high SUMO2/3 conjugation was prolonged in cells lacking sufficient chaperones. Similar results were obtained upon inhibiting HSP90, indicating that increased chaperone activity during the HSR is critical for recovery to normal SUMO2/3 levels post-heat shock. Proteasome inhibition likewise prolonged SUMO2/3 conjugation, indicating that stress-induced SUMO2/3 targets are subsequently degraded by the ubiquitin-proteasome system. Functionally, we suggest that SUMOylation can enhance the solubility of target proteins upon heat shock, a phenomenon that we experimentally observed in vitro. Collectively, our results implicate SUMO2/3 as a rapid response factor that coordinates proteome degradation and assists the maintenance of proteostasis upon proteotoxic stress.

Indexed as

Heat-Shock ResponseHeat Shock Transcription FactorsHEK293 CellsHumansMolecular ChaperonesProteomicsProteostasisSmall Ubiquitin-Related Modifier ProteinsSumoylationUbiquitinsHeat Shock Transcription FactorsHSF1 protein, humanMolecular ChaperonesSmall Ubiquitin-Related Modifier ProteinsSUMO2 protein, humanSUMO3 protein, humanUbiquitinschaperoneheat shock factor 1heat shock responseHSP90proteasomeproteostasisproteotoxic stresssmall ubiquitin-like modifierSUMO2/3ubiquitin

Identifiers

PMID30605679
PMCPMC6316133
OpenAlexW2907177719

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.