Evidence map›Paper›PMID 22853893›Full record

ReviewBiophysical journal2012

Sensing and responding to membrane tension: the bacterial MscL channel as a model system.

Irene Iscla, Paul Blount

Abstract readReview
In one paragraph

Review in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
  2. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026
    Review
  3. Effects ofMicroorganisms · 2024
    Article
  4. Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024
    Article
  5. Modeling membrane geometries implicitly in Rosetta.Protein science : a publication of the Protein Society · 2024
    Article
  6. Macromolecular crowding: Sensing without a sensor.Current opinion in cell biology · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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

2 authors.

Irene IsclaDepartment of Physiology, UT Southwestern Medical Center at Dallas, Dallas, Texas. USA.
Paul Blount

Funding

MOLECULAR MECHANISMS OF MECHANOSENSITIVE CHANNEL GATINGR01GM061028 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BLOUNT, PAUL · 2000 to 2017
$4.7M
High Throughput Screening: Bacterial Mechanosensitive Channels as Drug TargetsR03AI080807 · NIAID · UT SOUTHWESTERN MEDICAL CENTER · PI BLOUNT, PAUL · 2009 to 2010
$157k
NIAID NIH HHS AI080807NIAID NIH HHS R03 AI080807NIGMS NIH HHS GM061028NIGMS NIH HHS R01 GM061028
6 · The paper itself

Abstract

Mechanosensors are important for many life functions, including the senses of touch, balance, and proprioception; cardiovascular regulation; kidney function; and osmoregulation. Many channels from an assortment of families are now candidates for eukaryotic mechanosensors and proprioception, as well as cardiovascular regulation, kidney function, and osmoregulation. Bacteria also possess two families of mechanosensitive channels, termed MscL and MscS, that function as osmotic emergency release valves. Of the two channels, MscL is the most conserved, most streamlined in structure, and largest in conductance at 3.6 nS with a pore diameter in excess of 30 Å; hence, the structural changes required for gating are exaggerated and perhaps more easily defined. Because of these properties, as well as its tractable nature, MscL represents a excellent model for studying how a channel can sense and respond to biophysical changes of a lipid bilayer. Many of the properties of the MscL channel, such as the sensitivity to amphipaths, a helix that runs along the membrane surface and is connected to the pore via a glycine, a twisting and turning of the transmembrane domains upon gating, and the dynamic changes in membrane interactions, may be common to other candidate mechanosensors. Here we review many of these properties and discuss their structural and functional implications.

Indexed as

Mechanotransduction, CellularModels, BiologicalPressureBacterial ProteinsIon ChannelsProtein Structure, SecondaryBacterial ProteinsIon Channels

Identifiers

PMID22853893
PMCPMC3400780

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.