Evidence map›Paper›PMID 18341289›Full record

ArticleBiochemistry2008

Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL.

Andrew M Powl, J Malcolm East, Anthony G Lee

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024
    Article
  4. Review
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  14. Article
  15. Article
  16. Electrostatics at the membrane define MscL channel mechanosensitivity and kinetics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2014
    Article
  17. Article
  18. Article
  19. Article
  20. Helical membrane protein conformations and their environment.European biophysics journal : EBJ · 2013
    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

3 authors at 1 institution in 1 country.

Andrew M PowlSchool of Biological Sciences, University of Southampton, Southampton, SO16 7PX, UK.
J Malcolm East
Anthony G Lee
University of Southampton · GB

Funding

Wellcome Trust 076762
6 · The paper itself

Abstract

The mechanosensitive channel of large conductance MscL from Escherichia coli has been reconstituted into sealed vesicles, and the effects of lipid structure on the flux of the fluorescent molecule calcein through the open channel have been studied. The channel was opened by reaction of the G22C mutant of MscL with the reagent [2-(triethylammonium)ethyl]methanethiosulfonate (MTSET) which introduces five positive charges within the pore constriction. Flux through the channel was small when the lipid was phosphatidylcholine, but addition of the anionic lipids phosphatidylglycerol, phosphatidic acid, or cardiolipin up to 50 mol % resulted in increases in the amplitudes and rates of release of calcein. Similar effects were seen when either wild-type MscL or the G22C mutant was opened by osmotic pressure difference; rates of release of calcein were very slow in the absence of anionic lipid but increased with increasing concentrations of phosphatidylglycerol to 50 mol %. The observed partial release of trapped calcein following activation of MscL was attributed to the formation of a long-lived subconductance state of MscL following channel opening. Effects of anionic lipid were attributed to an increase in the rate of the transition from closed to fully open state and to a decrease in the rate of the transition from the fully open state to the subconductance state. Higher concentrations of anionic lipid led to a decrease in the rate and amplitude of release of calcein, possibly due to a decreased rate of flux through the open channel. In mixtures with anionic lipids, phosphatidylethanolamine resulted in lower rates and amplitude of release than phosphatidylcholine.

Indexed as

Escherichia coliAnionsEscherichia coli ProteinsFluoresceinsIon ChannelsMutationOsmotic PressurePhospholipidsSpectrometry, Mass, Electrospray IonizationAnionsEscherichia coli ProteinsFluoresceinsfluorexonIon ChannelsMscL protein, E coliPhospholipids

Identifiers

PMID18341289
PMCPMC2566799
OpenAlexW1997413922

What OpenQuestion holds

Textmetadata
LicenceTDM
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.