Evidence map›Paper›PMID 24859800›Full record

ReviewPflugers Archiv : European journal of physiology2015

MscL: channeling membrane tension.

Troy A Walton, Chinenye A Idigo, Nadia Herrera, Douglas C Rees

Abstract readReview
In one paragraph

Review in Pflugers Archiv : European journal of physiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Sonogenetics in the Treatment of Chronic Diseases: A New Method for Cell Regulation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Molecular Paradigms for Biological Mechanosensing.The journal of physical chemistry. B · 2021
    Article
  11. Article
  12. Review
  13. [Application of mechanosensitive channels in sonogenetics].Zhejiang da xue xue bao. Yi xue ban = Journal of Zhejiang University. Medical sciences · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  18. Article
  19. A special issue on physiological aspects of mechanosensing.Pflugers Archiv : European journal of physiology · 2015
    Article
  20. Review
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.

Troy A WaltonDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA, 91125, USA.
Chinenye A Idigo
Nadia Herrera
Douglas C Rees

Funding

PREDOCTORAL TRAINING IN BIOLOGY AND CHEMISTRYT32GM007616 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STERNBERG, PAUL WARREN · 1985 to 2019
$22.9M
Biophysical, Structural and Functional Analysis of Mechanosensitive ChannelsR01GM084211 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HASWELL, ELIZABETH S, PHILLIPS, ROB · 2008 to 2016
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM84211NIGMS NIH HHS R01 GM084211NIGMS NIH HHS T32 GM007616NIGMS NIH HHS T32 GM07616
6 · The paper itself

Abstract

Mechanosensitive channels are integral components for the response of bacteria to osmotic shock. The mechanosensitive channel of large conductance (MscL) responds to extreme turgor pressure increase that would otherwise lyse the cellular membrane. MscL has been studied as a model mechanosensitive channel using both structural and functional approaches. We will summarize the structural data and discuss outstanding questions surrounding the gating mechanism of this homo-oligomeric channel that has ~3 nS conductance. Specifically, we will explore the following: (1) the variability in oligomeric state that has been observed, (2) the open pore size measurements, and (3) the role of the C-terminal coiled coil domain for channel function. The oligomeric state of MscL has been characterized using various techniques, with a pentamer being the predominant form; however, the presence of mixtures of oligomers in the membrane is still uncertain. In the absence of structural data for the open state of MscL, the diameter of the open state pore has been estimated by several different approaches, leading to a current estimate between 25 and 30 Å. While the C-terminal domain is highly conserved among MscL homologues, it is not required for activity in vivo or in vitro. This domain is likely to remain intact during the gating transition and perform a filtering function that retains valuable osmolytes in the cytosol. Overall, studies of MscL have provided significant insight to the field, and serve as a paradigm for the analysis of non-homologous, eukaryotic mechanosensitive channel proteins.

Indexed as

Cell MembraneComputer SimulationEscherichia coli ProteinsIon Channel GatingIon ChannelsMechanotransduction, CellularMembrane FluidityModels, ChemicalModels, MolecularOsmoregulationPorosityStructure-Activity RelationshipEscherichia coli ProteinsIon ChannelsMscL protein, E coli

Identifiers

PMID24859800
PMCPMC4246047

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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.