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Nonmuscle myosin-2: mix and match

Members of the nonmuscle myosin-2 (NM-2) family of actin-based molecular motors catalyze the conversion of chemical energy into directed movement and force thereby acting as central regulatory components of the eukaryotic cytoskeleton. By cyclically interacting with adenosine triphosphate and F-acti...

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Detalles Bibliográficos
Autores principales: Heissler, Sarah M., Manstein, Dietmar J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: SP Birkhäuser Verlag Basel 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3535348/
https://www.ncbi.nlm.nih.gov/pubmed/22565821
http://dx.doi.org/10.1007/s00018-012-1002-9
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author Heissler, Sarah M.
Manstein, Dietmar J.
author_facet Heissler, Sarah M.
Manstein, Dietmar J.
author_sort Heissler, Sarah M.
collection PubMed
description Members of the nonmuscle myosin-2 (NM-2) family of actin-based molecular motors catalyze the conversion of chemical energy into directed movement and force thereby acting as central regulatory components of the eukaryotic cytoskeleton. By cyclically interacting with adenosine triphosphate and F-actin, NM-2 isoforms promote cytoskeletal force generation in established cellular processes like cell migration, shape changes, adhesion dynamics, endo- and exo-cytosis, and cytokinesis. Novel functions of the NM-2 family members in autophagy and viral infection are emerging, making NM-2 isoforms regulators of nearly all cellular processes that require the spatiotemporal organization of cytoskeletal scaffolding. Here, we assess current views about the role of NM-2 isoforms in these activities including the tight regulation of NM-2 assembly and activation through phosphorylation and how NM-2-mediated changes in cytoskeletal dynamics and mechanics affect cell physiological functions in health and disease.
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spelling pubmed-35353482013-01-04 Nonmuscle myosin-2: mix and match Heissler, Sarah M. Manstein, Dietmar J. Cell Mol Life Sci Review Members of the nonmuscle myosin-2 (NM-2) family of actin-based molecular motors catalyze the conversion of chemical energy into directed movement and force thereby acting as central regulatory components of the eukaryotic cytoskeleton. By cyclically interacting with adenosine triphosphate and F-actin, NM-2 isoforms promote cytoskeletal force generation in established cellular processes like cell migration, shape changes, adhesion dynamics, endo- and exo-cytosis, and cytokinesis. Novel functions of the NM-2 family members in autophagy and viral infection are emerging, making NM-2 isoforms regulators of nearly all cellular processes that require the spatiotemporal organization of cytoskeletal scaffolding. Here, we assess current views about the role of NM-2 isoforms in these activities including the tight regulation of NM-2 assembly and activation through phosphorylation and how NM-2-mediated changes in cytoskeletal dynamics and mechanics affect cell physiological functions in health and disease. SP Birkhäuser Verlag Basel 2012-05-08 2013 /pmc/articles/PMC3535348/ /pubmed/22565821 http://dx.doi.org/10.1007/s00018-012-1002-9 Text en © The Author(s) 2012 https://creativecommons.org/licenses/by/4.0/ This article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited.
spellingShingle Review
Heissler, Sarah M.
Manstein, Dietmar J.
Nonmuscle myosin-2: mix and match
title Nonmuscle myosin-2: mix and match
title_full Nonmuscle myosin-2: mix and match
title_fullStr Nonmuscle myosin-2: mix and match
title_full_unstemmed Nonmuscle myosin-2: mix and match
title_short Nonmuscle myosin-2: mix and match
title_sort nonmuscle myosin-2: mix and match
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3535348/
https://www.ncbi.nlm.nih.gov/pubmed/22565821
http://dx.doi.org/10.1007/s00018-012-1002-9
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