期刊
NATURE CELL BIOLOGY
卷 19, 期 2, 页码 133-141出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb3466
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资金
- Gordon and Betty Foundation
- Howard Hughes Medical Institute
- National Research Foundation Singapore
- Ministry of Education of Singapore [R-714-006-006-271]
- Ministry of Education Tier2 grant [MOE2015-T2-1-045]
- Israel Science Foundation
- Schmidt Minerva Center
- US-Israel Binational Science Foundation
- Joseph Moss Professorial Chair in Biomedical Research at the Weizmann Institute of Science, Israel
Although myosin II filaments are known to exist in non-muscle cells(1-2), 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 60s) 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 FmnI3, cofilin1 and alpha-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.
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