Evidence map›Paper›PMID 25450806›Full record

ArticleBiochimica et biophysica acta2015

The mechanosensitive channel of small conductance (MscS) functions as a Jack-in-the box.

Hannah R Malcolm, Paul Blount, Joshua A Maurer

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

17 citing papers in PubMed, 34 citations in OpenAlex.

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  13. Phosphoinositol-4,5-Bisphosphate Regulates Auditory Hair-Cell Mechanotransduction-Channel Pore Properties and Fast Adaptation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
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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

3 authors at 3 institutions in 1 country.

Hannah R MalcolmDepartment of Chemistry, Washington University in St. Louis, MO 63130, USA; Department of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 76390, USA.
Paul BlountDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, TX 76390, USA. Electronic address: paul.blount@utsouthwestern.edu.
Joshua A MaurerDepartment of Chemistry, Washington University in St. Louis, MO 63130, USA. Electronic address: Joshua.Maurer@att.net.
Southwestern Medical Center · USThe University of Texas Southwestern Medical Center · USWashington University in St. Louis · US

Funding

MOLECULAR MECHANISMS OF MECHANOSENSITIVE CHANNEL GATINGR01GM061028 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI BLOUNT, PAUL · 2000 to 2017
$4.7M
NIGMS NIH HHS GM061028NIGMS NIH HHS R01 GM061028
6 · The paper itself

Abstract

Phenotypical analysis of the lipid interacting residues in the closed state of the mechanosensitive channel of small conductance (MscS) from Escherichia coli (E. coli) has previously shown that these residues are critical for channel function. In the closed state, mutation of individual hydrophobic lipid lining residues to alanine, thus reducing the hydrophobicity, resulted in phenotypic changes that were observable using in vivo assays. Here, in an analogous set of experiments, we identify eleven residues in the first transmembrane domain of the open state of MscS that interact with the lipid bilayer. Each of these residues was mutated to alanine and leucine to modulate their hydrophobic interaction with the lipid tail-groups in the open state. The effects of these changes on channel function were analyzed using in vivo bacterial assays and patch clamp electrophysiology. Mutant channels were found to be functionally indistinguishable from wildtype MscS. Thus, mutation of open-state lipid interacting residues does not differentially stabilize or destabilize the open, closed, intermediate, or transition states of MscS. Based on these results and other data from the literature, we propose a new gating paradigm for MscS where MscS acts as a "Jack-In-The-Box" with the intrinsic bilayer lateral pressure holding the channel in the closed state. In this model, upon application of extrinsic tension the channel springs into the open state due to relief of the intrinsic lipid bilayer pressure.

Indexed as

Binding SitesEscherichia coliEscherichia coli ProteinsIon Channel GatingIon ChannelsLipid BilayersMechanotransduction, CellularMembrane PotentialsModels, MolecularMutationPatch-Clamp TechniquesPressureProtein BindingProtein Structure, TertiarySpheroplastsEscherichia coli ProteinsIon ChannelsLipid BilayersMscS protein, E coliBacterial ion channelGating mechanismJack-In-The-BoxLipid interactionMechanosensitive channel of small conductance (MscS)

Identifiers

PMID25450806
PMCPMC4259861
OpenAlexW2078532646

What OpenQuestion holds

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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.