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Contraction Mechanisms in Composite Active Actin Networks
Simplified in vitro systems are ideally suited for studying the principle mechanisms of the contraction of cytoskeletal actin systems. To shed light on the dependence of the contraction mechanism on the nature of the crosslinking proteins, we study reconstituted in vitro active actin networks on dif...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388086/ https://www.ncbi.nlm.nih.gov/pubmed/22768316 http://dx.doi.org/10.1371/journal.pone.0039869 |
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author | Köhler, Simone Bausch, Andreas R. |
author_facet | Köhler, Simone Bausch, Andreas R. |
author_sort | Köhler, Simone |
collection | PubMed |
description | Simplified in vitro systems are ideally suited for studying the principle mechanisms of the contraction of cytoskeletal actin systems. To shed light on the dependence of the contraction mechanism on the nature of the crosslinking proteins, we study reconstituted in vitro active actin networks on different length scales ranging from the molecular organization to the macroscopic contraction. Distinct contraction mechanisms are observed in polar and apolar crosslinked active gels whereas composite active gels crosslinked in a polar and apolar fashion at the same time exhibit both mechanisms simultaneously. In polar active actin/fascin networks initially bundles are formed which are then rearranged. In contrast, apolar cortexillin-I crosslinked active gels are bundled only after reorganization of actin filaments by myosin-II motor filaments. |
format | Online Article Text |
id | pubmed-3388086 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-33880862012-07-05 Contraction Mechanisms in Composite Active Actin Networks Köhler, Simone Bausch, Andreas R. PLoS One Research Article Simplified in vitro systems are ideally suited for studying the principle mechanisms of the contraction of cytoskeletal actin systems. To shed light on the dependence of the contraction mechanism on the nature of the crosslinking proteins, we study reconstituted in vitro active actin networks on different length scales ranging from the molecular organization to the macroscopic contraction. Distinct contraction mechanisms are observed in polar and apolar crosslinked active gels whereas composite active gels crosslinked in a polar and apolar fashion at the same time exhibit both mechanisms simultaneously. In polar active actin/fascin networks initially bundles are formed which are then rearranged. In contrast, apolar cortexillin-I crosslinked active gels are bundled only after reorganization of actin filaments by myosin-II motor filaments. Public Library of Science 2012-07-02 /pmc/articles/PMC3388086/ /pubmed/22768316 http://dx.doi.org/10.1371/journal.pone.0039869 Text en Köhler, Bausch. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Köhler, Simone Bausch, Andreas R. Contraction Mechanisms in Composite Active Actin Networks |
title | Contraction Mechanisms in Composite Active Actin Networks |
title_full | Contraction Mechanisms in Composite Active Actin Networks |
title_fullStr | Contraction Mechanisms in Composite Active Actin Networks |
title_full_unstemmed | Contraction Mechanisms in Composite Active Actin Networks |
title_short | Contraction Mechanisms in Composite Active Actin Networks |
title_sort | contraction mechanisms in composite active actin networks |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3388086/ https://www.ncbi.nlm.nih.gov/pubmed/22768316 http://dx.doi.org/10.1371/journal.pone.0039869 |
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