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  Myosin-II activity generates a dynamic steady state with continuous actin turnover in a minimal actin cortex.

Sonal, Ganzinger, K. A., Vogel, S. K., Mücksch, J., Blumhardt, P., & Schwille, P. (2018). Myosin-II activity generates a dynamic steady state with continuous actin turnover in a minimal actin cortex. Journal of Cell Science, 132(4): jcs219899. doi:10.1242/jcs.219899.

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© 2018. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/4.0This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
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 Creators:
Sonal1, Author              
Ganzinger, Kristina A.1, Author              
Vogel, Sven K.1, Author              
Mücksch, Jonas1, Author              
Blumhardt, Philipp1, Author              
Schwille, Petra1, Author              
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              

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Free keywords: Cytoskeletal dynamics; In vitro reconstitution; Supported lipid bilayer; Synthetic biology; WASP
 Abstract: Dynamic reorganization of the actomyosin cytoskeleton allows fast modulation of the cell surface, which is vital for many cellular functions. Myosin-II motors generate the forces required for this remodeling by imparting contractility to actin networks. However, myosin-II activity might also have a more indirect contribution to cytoskeletal dynamics; it has been proposed that myosin activity increases actin turnover in various cellular contexts, presumably by enhancing disassembly. In vitro reconstitution of actomyosin networks has confirmed the role of myosin in actin network disassembly, but the reassembly of actin in these assays was limited by factors such as diffusional constraints and the use of stabilized actin filaments. Here, we present the reconstitution of a minimal dynamic actin cortex, where actin polymerization is catalyzed on the membrane in the presence of myosin-II activity. We demonstrate that myosin activity leads to disassembly and redistribution in this simplified cortex. Consequently, a new dynamic steady state emerges in which the actin network undergoes constant turnover. Our findings suggest a multifaceted role of myosin-II in the dynamics of the eukaryotic actin cortex. This article has an associated First Person interview with the first author of the paper. © 2018. Published by The Company of Biologists Ltd.

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Language(s): eng - English
 Dates: 2018-12-112018
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 30538127
DOI: 10.1242/jcs.219899
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Project name : -
Grant ID : 703132
Funding program : Horizon 2020 (H2020)
Funding organization : European Commission (EC)

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Title: Journal of Cell Science
Source Genre: Journal
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Publ. Info: Cambridge, U.K. : Co. of Biologists
Pages: - Volume / Issue: 132 (4) Sequence Number: jcs219899 Start / End Page: - Identifier: ISSN: 0021-9533
CoNE: https://pure.mpg.de/cone/journals/resource/954925326678