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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...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SP Birkhäuser Verlag Basel
2012
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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. |
format | Online Article Text |
id | pubmed-3535348 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | SP Birkhäuser Verlag Basel |
record_format | MEDLINE/PubMed |
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 |
work_keys_str_mv | AT heisslersarahm nonmusclemyosin2mixandmatch AT mansteindietmarj nonmusclemyosin2mixandmatch |