Nuclear myosin I regulates cell membrane tension
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...
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pubmed-49696042016-08-11 Nuclear myosin I regulates cell membrane tension Venit, Tomáš Kalendová, Alžběta Petr, Martin Dzijak, Rastislav Pastorek, Lukáš Rohožková, Jana Malohlava, Jakub Hozák, Pavel Article 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. Nature Publishing Group 2016-08-02 /pmc/articles/PMC4969604/ /pubmed/27480647 http://dx.doi.org/10.1038/srep30864 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
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Open Access Journal |
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Foreign Institution |
institution |
US National Center for Biotechnology Information |
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NCBI PubMed |
collection |
Online Access |
language |
English |
format |
Online |
author |
Venit, Tomáš Kalendová, Alžběta Petr, Martin Dzijak, Rastislav Pastorek, Lukáš Rohožková, Jana Malohlava, Jakub Hozák, Pavel |
spellingShingle |
Venit, Tomáš Kalendová, Alžběta Petr, Martin Dzijak, Rastislav Pastorek, Lukáš Rohožková, Jana Malohlava, Jakub Hozák, Pavel Nuclear myosin I regulates cell membrane tension |
author_facet |
Venit, Tomáš Kalendová, Alžběta Petr, Martin Dzijak, Rastislav Pastorek, Lukáš Rohožková, Jana Malohlava, Jakub Hozák, Pavel |
author_sort |
Venit, Tomáš |
title |
Nuclear myosin I regulates cell membrane tension |
title_short |
Nuclear myosin I regulates cell membrane tension |
title_full |
Nuclear myosin I regulates cell membrane tension |
title_fullStr |
Nuclear myosin I regulates cell membrane tension |
title_full_unstemmed |
Nuclear myosin I regulates cell membrane tension |
title_sort |
nuclear myosin i regulates cell membrane tension |
description |
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. |
publisher |
Nature Publishing Group |
publishDate |
2016 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4969604/ |
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1613619221403533312 |