Myosin II Filament Dynamics in Actin Networks Revealed with Interferometric Scattering Microscopy.

Autor:	Mosby LS; Centre for Mechanochemical Cell Biology, University of Warwick, Coventry, United Kingdom; Physics Department, University of Warwick, Coventry, United Kingdom., Hundt N; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom., Young G; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom., Fineberg A; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom., Polin M; Centre for Mechanochemical Cell Biology, University of Warwick, Coventry, United Kingdom; Physics Department, University of Warwick, Coventry, United Kingdom., Mayor S; National Centre for Biological Sciences, Tata Institute for Fundamental Research, Bangalore, India; Institute for Stem Cell Biology and Regenerative Medicine, Bangalore, India. Electronic address: mayor@ncbs.res.in., Kukura P; Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford, United Kingdom. Electronic address: philipp.kukura@chem.ox.ac.uk., Köster DV; Centre for Mechanochemical Cell Biology, University of Warwick, Coventry, United Kingdom; Division of Biomedical Sciences, Warwick Medical School, University of Warwick, Coventry, United Kingdom. Electronic address: d.koester@warwick.ac.uk.
Jazyk:	angličtina
Zdroj:	Biophysical journal [Biophys J] 2020 Apr 21; Vol. 118 (8), pp. 1946-1957. Date of Electronic Publication: 2020 Mar 04.
DOI:	10.1016/j.bpj.2020.02.025
Abstrakt:	The plasma membrane and the underlying cytoskeletal cortex constitute active platforms for a variety of cellular processes. Recent work has shown that the remodeling acto-myosin network modifies local membrane organization, but the molecular details are only partly understood because of difficulties with experimentally accessing the relevant time and length scales. Here, we use interferometric scattering microscopy to investigate a minimal acto-myosin network linked to a supported lipid bilayer membrane. Using the magnitude of the interferometric contrast, which is proportional to molecular mass, and fast acquisition rates, we detect and image individual membrane-attached actin filaments diffusing within the acto-myosin network and follow individual myosin II filament dynamics. We quantify myosin II filament dwell times and processivity as functions of ATP concentration, providing experimental evidence for the predicted ensemble behavior of myosin head domains. Our results show how decreasing ATP concentrations lead to both increasing dwell times of individual myosin II filaments and a global change from a remodeling to a contractile state of the acto-myosin network. (Copyright © 2020 Biophysical Society. Published by Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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