TY - JOUR
T1 - Long-range self-organization of cytoskeletal myosin II filament stacks
AU - Hu, Shiqiong
AU - Dasbiswas, Kinjal
AU - Guo, Zhenhuan
AU - Tee, Yee-Han
AU - Thiagarajan, Visalatchi
AU - Hersen, Pascal
AU - Chew, Teng-Leong
AU - Safran, Samuel
AU - Zaidel-Bar, Ronen
AU - Bershadsky, Alexander D.
N1 - Publisher Copyright: © 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved.
PY - 2017/1/31
Y1 - 2017/1/31
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85010880256&partnerID=8YFLogxK
U2 - https://doi.org/10.1038/ncb3466
DO - https://doi.org/10.1038/ncb3466
M3 - مقالة
SN - 1465-7392
VL - 19
SP - 133
EP - 141
JO - Nature Cell Biology
JF - Nature Cell Biology
IS - 2
ER -