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Nuclear myosin I regulates cell membrane tension
T. Venit, A. Kalendová, M. Petr, R. Dzijak, L. Pastorek, J. Rohožková, J. Malohlava, P. Hozák,
Language English Country England, Great Britain
Document type Journal Article, Research Support, Non-U.S. Gov't
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PubMed
27480647
DOI
10.1038/srep30864
Knihovny.cz E-resources
- MeSH
- Cell Membrane metabolism MeSH
- Cell Nucleus metabolism MeSH
- Exocytosis physiology MeSH
- Fibroblasts cytology metabolism MeSH
- HeLa Cells MeSH
- Cells, Cultured MeSH
- Skin cytology metabolism MeSH
- Humans MeSH
- Actin Cytoskeleton metabolism MeSH
- Myosin Type I metabolism MeSH
- Mice, Knockout MeSH
- Mice MeSH
- Cell Movement MeSH
- Cell Shape MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
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.
References provided by Crossref.org
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