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Nat Cell Biol. 2017 Feb;19(2):133-141. doi: 10.1038/ncb3466. Epub 2017 Jan 23.

Long-range self-organization of cytoskeletal myosin II filament stacks.

Author information

1
Mechanobiology Institute, National University of Singapore, Singapore 117411, Singapore.
2
Department of Materials and Interfaces, Weizmann Institute of Science, Rehovot 76100, Israel.
3
James Franck Institute, University of Chicago, Chicago, Illinois 60637, USA.
4
Laboratoire Matire et Systèmes Complexes, UMR 7057 CNRS &Université Paris Diderot, Paris 75013, France.
5
Advanced Imaging Center, HHMI Janelia Research Campus, Ashburn, Virginia 20147, USA.
6
Department of Molecular Cell Biology, Weizmann Institute of Science, Rehovot 76100, Israel.

Abstract

Although myosin II filaments are known to exist in non-muscle cells, their dynamics and organization are incompletely understood. Here, we combined structured illumination microscopy with pharmacological and genetic perturbations, to study the process of actomyosin cytoskeleton self-organization into arcs and stress fibres. A striking feature of the myosin II filament organization was their 'registered' alignment into stacks, spanning up to several micrometres in the direction orthogonal to the parallel actin bundles. While turnover of individual myosin II filaments was fast (characteristic half-life time 60 s) and independent of actin filament turnover, the process of stack formation lasted a longer time (in the range of several minutes) and required myosin II contractility, as well as actin filament assembly/disassembly and crosslinking (dependent on formin Fmnl3, cofilin1 and α-actinin-4). Furthermore, myosin filament stack formation involved long-range movements of individual myosin filaments towards each other suggesting the existence of attractive forces between myosin II filaments. These forces, possibly transmitted via mechanical deformations of the intervening actin filament network, may in turn remodel the actomyosin cytoskeleton and drive its self-organization.

PMID:
28114270
DOI:
10.1038/ncb3466
[Indexed for MEDLINE]

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