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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Main Authors: Venit, Tomáš, Kalendová, Alžběta, Petr, Martin, Dzijak, Rastislav, Pastorek, Lukáš, Rohožková, Jana, Malohlava, Jakub, Hozák, Pavel
Format: Online
Language:English
Published: Nature Publishing Group 2016
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4969604/
id pubmed-4969604
recordtype oai_dc
spelling 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/
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building 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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