Evidence map›Paper›PMID 29196524›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Protein kinase C and calcineurin cooperatively mediate cell survival under compressive mechanical stress.

Ranjan Mishra, Frank van Drogen, Reinhard Dechant, Soojung Oh, Noo Li Jeon, Sung Sik Lee, Matthias Peter

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing 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

22 citing papers in PubMed.

  1. Article
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  5. Article
  6. Cip1 tunes cell cycle arrest duration upon calcineurin activation.Proceedings of the National Academy of Sciences of the United States of America · 2022
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  7. Article
  8. Review
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  11. Article
  12. Mechanism of Candida pathogenesis: revisiting the vital drivers.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2020
    Review
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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

7 authors.

Ranjan MishraInstitute of Biochemistry, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland.
Frank van DrogenInstitute of Biochemistry, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland.
Reinhard DechantInstitute of Biochemistry, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland.ORCID 0000-0002-4094-4773
Soojung OhDepartment of Mechanical & Aerospace Engineering, Seoul National University, 08826 Seoul, Republic of Korea.
Noo Li JeonDepartment of Mechanical & Aerospace Engineering, Seoul National University, 08826 Seoul, Republic of Korea.
Sung Sik LeeInstitute of Biochemistry, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland; sungsik.lee@scopem.ethz.ch matthias.peter@bc.biol.ethz.ch.ORCID 0000-0001-9267-232X
Matthias PeterInstitute of Biochemistry, Department of Biology, ETH Zürich, 8093 Zürich, Switzerland; sungsik.lee@scopem.ethz.ch matthias.peter@bc.biol.ethz.ch.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cells experience compressive stress while growing in limited space or migrating through narrow constrictions. To survive such stress, cells reprogram their intracellular organization to acquire appropriate mechanical properties. However, the mechanosensors and downstream signaling networks mediating these changes remain largely unknown. Here, we have established a microfluidic platform to specifically trigger compressive stress, and to quantitatively monitor single-cell responses of budding yeast in situ. We found that yeast senses compressive stress via the cell surface protein Mid2 and the calcium channel proteins Mid1 and Cch1, which then activate the Pkc1/Mpk1 MAP kinase pathway and calcium signaling, respectively. Genetic analysis revealed that these pathways work in parallel to mediate cell survival. Mid2 contains a short intracellular tail and a serine-threonine-rich extracellular domain with spring-like properties, and both domains are required for mechanosignaling. Mid2-dependent spatial activation of the Pkc1/Mpk1 pathway depolarizes the actin cytoskeleton in budding or shmooing cells, thereby antagonizing polarized growth to protect cells under compressive stress conditions. Together, these results identify a conserved signaling network responding to compressive mechanical stress, which, in higher eukaryotes, may ensure cell survival in confined environments.

Indexed as

Stress, MechanicalActin CytoskeletonCalcineurinCalcium ChannelsCalcium SignalingCell SurvivalCell WallIntracellular Signaling Peptides and ProteinsMAP Kinase Signaling SystemMechanotransduction, CellularMembrane GlycoproteinsMicrofluidicsMitogen-Activated Protein KinasesProtein Kinase CSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCalcineurinCalcium ChannelsCCH1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsMembrane GlycoproteinsMID1 protein, S cerevisiaeMID2 protein, S cerevisiaeMitogen-Activated Protein KinasesPKC1 protein, S cerevisiaeProtein Kinase CSaccharomyces cerevisiae ProteinsSLT2 protein, S cerevisiaecalcium signalingcell polaritymechanosensormicrofluidicsPkc1/Mpk1 pathway

Identifiers

PMID29196524
PMCPMC5754771

What OpenQuestion holds

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Registered trials

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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.