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  Interplay between myosin II and actin dynamics in chemotactic amoeba

Hsu, H.-F., Krekhov, A., Tarantola, M., Beta, C., & Bodenschatz, E. (2019). Interplay between myosin II and actin dynamics in chemotactic amoeba. New Journal of Physics, 21: 113055. doi:10.1088/1367-2630/ab5822.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0005-D939-7 Version Permalink: http://hdl.handle.net/21.11116/0000-0005-D93A-6
Genre: Journal Article

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 Creators:
Hsu, Hsin-Fang1, Author              
Krekhov, Alexei1, Author              
Tarantola, Marco1, Author              
Beta, Carsten1, Author              
Bodenschatz, Eberhard1, Author              
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1Laboratory for Fluid Dynamics, Pattern Formation and Biocomplexity, Max Planck Institute for Dynamics and Self-Organization, Max Planck Society, ou_2063287              

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 Abstract: The actin cytoskeleton and its response to external chemical stimuli is fundamental to the mechano-biology of eukaryotic cells and their functions. One of the key players that governs the dynamics of the actin network is the motor protein myosin II. Based on a phase space embedding we have identified from experiments three phases in the cytoskeletal dynamics of starved Dictyostelium discoideum in response to a precisely controlled chemotactic stimulation. In the first two phases the dynamics of actin and myosin II in the cortex is uncoupled, while in the third phase the time scale for the recovery of cortical actin is determined by the myosin II dynamics. We report a theoretical model that captures the experimental observations quantitatively. The model predicts an increase in the optimal response time of actin with decreasing myosin II-actin coupling strength highlighting the role of myosin II in the robust control of cell contraction.

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Language(s): eng - English
 Dates: 2019-11-282019-11
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1088/1367-2630/ab5822
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Title: New Journal of Physics
Source Genre: Journal
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Pages: 15 Volume / Issue: 21 Sequence Number: 113055 Start / End Page: - Identifier: -