Evidence map›Paper›PMID 27480647›Full record

ArticleScientific reports2016

Nuclear myosin I regulates cell membrane tension.

Tomáš Venit, Alžběta Kalendová, Martin Petr, Rastislav Dzijak, Lukáš Pastorek, Jana Rohožková, Jakub Malohlava, Pavel Hozák

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. 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 19% 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, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Liraglutide Promotes Diabetic Wound Healing via Myo1c/Dock5.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Targeting myosin 1c inhibits murine hepatic fibrogenesis.American journal of physiology. Gastrointestinal and liver physiology · 2021
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. N-terminal splicing extensions of the humanThe Journal of biological chemistry · 2017
    Article
  16. Article
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

8 authors at 3 institutions in 1 country.

Tomáš VenitDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Alžběta KalendováDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Martin PetrDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Rastislav DzijakDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Lukáš PastorekDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Jana RohožkováDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Jakub MalohlavaDepartment of Medical Biophysics, Faculty of Medicine and Dentistry, Palacky University in Olomouc, Hnevotinska 3, 775 15 Olomouc, Czech Republic.
Pavel HozákDepartment of Biology of the Cell Nucleus, Institute of Molecular Genetics, AS CR, v.v.i., Videnska 1083, 142 20 Prague, Czech Republic.
Czech Academy of Sciences, Institute of Molecular Genetics · CZCharles University · CZPalacký University Olomouc · CZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plasma membrane tension is an important feature that determines the cell shape and influences processes such as cell motility, spreading, endocytosis and exocytosis. Unconventional class 1 myosins are potent regulators of plasma membrane tension because they physically link the plasma membrane with adjacent cytoskeleton. We identified nuclear myosin 1 (NM1) - a putative nuclear isoform of myosin 1c (Myo1c) - as a new player in the field. Although having specific nuclear functions, NM1 localizes predominantly to the plasma membrane. Deletion of NM1 causes more than a 50% increase in the elasticity of the plasma membrane around the actin cytoskeleton as measured by atomic force microscopy. This higher elasticity of NM1 knock-out cells leads to 25% higher resistance to short-term hypotonic environment and rapid cell swelling. In contrast, overexpression of NM1 in wild type cells leads to an additional 30% reduction of their survival. We have shown that NM1 has a direct functional role in the cytoplasm as a dynamic linker between the cell membrane and the underlying cytoskeleton, regulating the degree of effective plasma membrane tension.

Indexed as

Actin CytoskeletonAnimalsCell MembraneCell MovementCell NucleusCells, CulturedCell ShapeExocytosisFibroblastsHeLa CellsHumansMiceMice, KnockoutMyosin Type ISkinMyosin Type I

Identifiers

PMID27480647
PMCPMC4969604
OpenAlexW2495369324

What OpenQuestion holds

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LicenceCC BY
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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.