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

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.

journal_name

Nat Cell Biol

journal_title

Nature cell biology

authors

Hu S,Dasbiswas K,Guo Z,Tee YH,Thiagarajan V,Hersen P,Chew TL,Safran SA,Zaidel-Bar R,Bershadsky AD

doi

10.1038/ncb3466

subject

Has Abstract

pub_date

2017-02-01 00:00:00

pages

133-141

issue

2

eissn

1465-7392

issn

1476-4679

pii

ncb3466

journal_volume

19

pub_type

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