Evidence map›Paper›PMID 26368283›Full record

ArticlePloS one2015

Scanning MscL Channels with Targeted Post-Translational Modifications for Functional Alterations.

Irene Iscla, Robin Wray, Christina Eaton, Paul Blount

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.5field-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

16 citing papers in PubMed, 24 citations in OpenAlex.

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  12. Novel compounds that specifically bind and modulate MscL: insights into channel gating mechanisms.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019
    Article
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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

4 authors at 1 institution in 1 country.

Irene IsclaDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas, United States of America.
Robin WrayDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas, United States of America.
Christina EatonDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas, United States of America.
Paul BlountDepartment of Physiology, University of Texas Southwestern Medical Center at Dallas, Dallas, Texas, United States of America.
The University of Texas Southwestern Medical Center · 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

Mechanosensitive channels are present in all living organisms and are thought to underlie the senses of touch and hearing as well as various important physiological functions like osmoregulation and vasoregulation. The mechanosensitive channel of large conductance (MscL) from Escherichia coli was the first protein shown to encode mechanosensitive channel activity and serves as a paradigm for how a channel senses and responds to mechanical stimuli. MscL plays a role in osmoprotection in E. coli, acting as an emergency release valve that is activated by membrane tension due to cell swelling after an osmotic down-shock. Using an osmotically fragile strain in an osmotic down-shock assay, channel functionality can be directly determined in vivo. In addition, using thiol reagents and expressed MscL proteins with a single cysteine substitution, we have shown that targeted post-translational modifications can be performed, and that any alterations that lead to dysfunctional proteins can be identified by this in vivo assay. Here, we present the results of such a scan performed on 113 MscL cysteine mutants using five different sulfhydryl-reacting probes to confer different charges or hydrophobicity to each site. We assessed which of these targeted modifications affected channel function and the top candidates were further studied using patch clamp to directly determine how channel activity was affected. This comprehensive screen has identified many residues that are critical for channel function as well as highlighted MscL domains and residues that undergo the most drastic environmental changes upon gating.

Indexed as

Amino Acid SubstitutionCysteineEscherichia coliEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsIon Channel GatingIon ChannelsMutation, MissenseOsmotic PressureProtein Processing, Post-TranslationalProtein Structure, TertiaryCysteineEscherichia coli ProteinsIon ChannelsMscL protein, E coli

Identifiers

PMID26368283
PMCPMC4569298
OpenAlexW2217173021

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.