Evidence map›Paper›PMID 28263768›Full record

ArticleJournal of molecular biology2017

Osmotic Shock Induced Protein Destabilization in Living Cells and Its Reversal by Glycine Betaine.

Samantha S Stadmiller, Annelise H Gorensek-Benitez, Alex J Guseman, Gary J Pielak

Abstract read
In one paragraph

Article in Journal of molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Crowding-induced stabilization and destabilization in a single protein.Protein science : a publication of the Protein Society · 2025
    Article
  5. Amino acids modulate liquid-liquid phase separation in vitro and in vivo by regulating protein-protein interactions.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Chemical interactions modulate λProtein science : a publication of the Protein Society · 2023
    Article
  14. Review
  15. Water Stress-Driven Changes in Bacterial Cell Surface Properties.Applied and environmental microbiology · 2022
    Article
  16. Review
  17. Review
  18. L-Proline Synthesis Mutants ofFrontiers in microbiology · 2022
    Article
  19. Review
  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

4 authors.

Samantha S StadmillerDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA.
Annelise H Gorensek-BenitezDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA.
Alex J GusemanDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA.
Gary J PielakDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC 27514, USA; Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, 120 Mason Farm Road, Chapel Hill, NC 27599, USA; Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, 101 Manning Drive, Chapel Hill, NC 27514, USA. Electronic address: gary_pielak@unc.edu.

Funding

MOLECULAR AND CELLULAR BIOPHYSICS TRAINING PROGRAMT32GM008570 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI KUHLMAN, BRIAN A, SLEP, KEVIN C · 1995 to 2022
$5.1M
NIGMS NIH HHS T32 GM008570
6 · The paper itself

Abstract

Many organisms can adapt to changes in the solute content of their surroundings (i.e., the osmolarity). Hyperosmotic shock causes water efflux and a concomitant reduction in cell volume, which is countered by the accumulation of osmolytes. This volume reduction increases the crowded nature of the cytoplasm, which is expected to affect protein stability. In contrast to traditional theory, which predicts that more crowded conditions can only increase protein stability, recent work shows that crowding can destabilize proteins through transient attractive interactions. Here, we quantify protein stability in living Escherichia coli cells before and after hyperosmotic shock in the presence and absence of the osmolyte, glycine betaine. The 7-kDa N-terminal src-homology 3 domain of Drosophila signal transduction protein drk is used as the test protein. We find that hyperosmotic shock decreases SH3 stability in cells, consistent with the idea that transient attractive interactions are important under physiologically relevant crowded conditions. The subsequent uptake of glycine betaine returns SH3 to the stability observed without osmotic shock. These results highlight the effect of transient attractive interactions on protein stability in cells and provide a new explanation for why stressed cells accumulate osmolytes.

Indexed as

Protein StabilityBetaineDrosophila ProteinsEscherichia coliMagnetic Resonance SpectroscopyOsmotic Pressuresrc Homology DomainsBetainedrk protein, DrosophilaDrosophila Proteinsglycine betaineosmolytesosmotic shockprotein NMRprotein stability

Identifiers

PMID28263768
PMCPMC5985519

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Registered trials

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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.