Evidence map›Paper›PMID 21613604›Full record

ArticleAmerican journal of physiology. Cell physiology2011

Hypertonic stress induces rapid and widespread protein damage in C. elegans.

Kris Burkewitz, Keith Choe, Kevin Strange

Abstract read
In one paragraph

Article in American journal of physiology. Cell physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing 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

47 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
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  7. Article
  8. Low humidity enhances thermotolerance inmicroPublication biology · 2024
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Stress increases in exopher-mediated neuronal extrusion require lipid biosynthesis, FGF, and EGF RAS/MAPK signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. The C. elegans Hypertonic Stress Response: Big Insights from Shrinking Worms.Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology · 2021
    Review
  17. Article
  18. Article
  19. Automated phenotyping ofMicrosystems & nanoengineering · 2020
    Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

3 authors.

Kris BurkewitzBoylan Center for Cellular and Molecular Physiology, Mount Desert Island Biological Laboratory, Salisbury Cove, Maine 04672, USA.
Keith Choe
Kevin Strange

Funding

Regulation of a C. elegans CIC channel by phosphorylation and membrane retrievalR01DK061168 · NIDDK · VANDERBILT UNIVERSITY · PI STRANGE, KEVIN · 2001 to 2013
$4.1M
NIDDK NIH HHS R01 DK61168
6 · The paper itself

Abstract

Proteostasis is defined as the homeostatic mechanisms that maintain the function of all cytoplasmic proteins. We recently demonstrated that the capacity of the proteostasis network is a critical factor that defines the limits of cellular and organismal survival in hypertonic environments. The current studies were performed to determine the extent of protein damage induced by cellular water loss. Using worm strains expressing fluorescently tagged foreign and endogenous proteins and proteins with temperature-sensitive point mutations, we demonstrate that hypertonic stress causes aggregation and misfolding of diverse proteins in multiple cell types. Protein damage is rapid. Aggregation of a polyglutamine yellow fluorescent protein reporter is observable with <1 h of hypertonic stress, and aggregate volume doubles approximately every 10 min. Aggregate formation is irreversible and occurs after as little as 10 min of exposure to hypertonic conditions. To determine whether endogenous proteins are aggregated by hypertonic stress, we quantified the relative amount of total cellular protein present in detergent-insoluble extracts. Exposure for 4 h to 400 mM or 500 mM NaCl induced a 55-120% increase in endogenous protein aggregation. Inhibition of insulin signaling or acclimation to mild hypertonic stress increased survival under extreme hypertonic conditions and prevented aggregation of endogenous proteins. Our results demonstrate that hypertonic stress causes widespread and dramatic protein damage and that cells have a significant capacity to remodel the network of proteins that function to maintain proteostasis. These findings have important implications for understanding how cells cope with hypertonic stress and other protein-damaging stressors.

Indexed as

Acclimatizationalpha-SynucleinAnimalsAnimals, Genetically ModifiedBacterial ProteinsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell NucleusForkhead Transcription FactorsGenes, ReporterInclusion BodiesInsulinLuminescent ProteinsMembrane ProteinsMovementMuscle Cellsalpha-SynucleinBacterial ProteinsCaenorhabditis elegans Proteinsdaf-16 protein, C elegansDAF-2 protein, C elegansForkhead Transcription FactorsInsulinKIN-19 protein, C eleganslet-60 protein, C elegansLuminescent ProteinsMembrane ProteinsPeptidespolyglutamineProtein KinasesProteoglycansras ProteinsReceptor, InsulinRecombinant Fusion ProteinsRed Fluorescent ProteinRNA, Double-StrandedSaline Solution, HypertonicTranscription FactorsTropomyosinUNC-15 protein, C elegansunc-52 protein, C elegansyellow fluorescent protein, Bacteria

Identifiers

PMID21613604
PMCPMC3174568

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.