Evidence map›Paper›PMID 25052715›Full record

ArticleThe Plant cell2014

Arabidopsis MSL10 has a regulated cell death signaling activity that is separable from its mechanosensitive ion channel activity.

Kira M Veley, Grigory Maksaev, Elizabeth M Frick, Emma January, Sarah C Kloepper, Elizabeth S Haswell

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
8.4field-weighted citation impact, top 3% 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

34 citing papers in PubMed, 84 citations in OpenAlex.

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  17. Cellular transduction of mechanical oscillations in plants by the plasma-membrane mechanosensitive channel MSL10.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

6 authors at 1 institution in 1 country.

Kira M VeleyDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Grigory MaksaevDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Elizabeth M FrickDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Emma JanuaryDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Sarah C KloepperDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Elizabeth S HaswellDepartment of Biology, Washington University, St. Louis, Missouri 63130 ehaswell@wustl.edu.
Washington University in St. Louis · US

Funding

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 GM084211NIGMS NIH HHS R01 GM084211
6 · The paper itself

Abstract

Members of the MscS superfamily of mechanosensitive ion channels function as osmotic safety valves, releasing osmolytes under increased membrane tension. MscS homologs exhibit diverse topology and domain structure, and it has been proposed that the more complex members of the family might have novel regulatory mechanisms or molecular functions. Here, we present a study of MscS-Like (MSL)10 from Arabidopsis thaliana that supports these ideas. High-level expression of MSL10-GFP in Arabidopsis induced small stature, hydrogen peroxide accumulation, ectopic cell death, and reactive oxygen species- and cell death-associated gene expression. Phosphomimetic mutations in the MSL10 N-terminal domain prevented these phenotypes. The phosphorylation state of MSL10 also regulated its ability to induce cell death when transiently expressed in Nicotiana benthamiana leaves but did not affect subcellular localization, assembly, or channel behavior. Finally, the N-terminal domain of MSL10 was sufficient to induce cell death in tobacco, independent of phosphorylation state. We conclude that the plant-specific N-terminal domain of MSL10 is capable of inducing cell death, this activity is regulated by phosphorylation, and MSL10 has two separable activities-one as an ion channel and one as an inducer of cell death. These findings further our understanding of the evolution and significance of mechanosensitive ion channels.

Indexed as

Signal TransductionArabidopsisArabidopsis ProteinsCell DeathEvolution, MolecularGene ExpressionGenes, ReporterHydrogen PeroxideIon ChannelsMembrane ProteinsModels, MolecularMutationNicotianaPhosphorylationPlant LeavesPlants, Genetically ModifiedArabidopsis ProteinsHydrogen PeroxideIon ChannelsMembrane ProteinsMSL10 protein, ArabidopsisReactive Oxygen SpeciesRecombinant Fusion Proteins

Identifiers

PMID25052715
PMCPMC4145136
OpenAlexW2147577454

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.