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Actin dynamics and competition for myosin monomer govern the sequential amplification of myosin filaments.


ABSTRACT: The cellular mechanisms governing non-muscle myosin II (NM2) filament assembly are largely unknown. Using EGFP-NM2A knock-in fibroblasts and multiple super-resolution imaging modalities, we characterized and quantified the sequential amplification of NM2 filaments within lamellae, wherein filaments emanating from single nucleation events continuously partition, forming filament clusters that populate large-scale actomyosin structures deeper in the cell. Individual partitioning events coincide spatially and temporally with the movements of diverging actin fibres, suppression of which inhibits partitioning. These and other data indicate that NM2A filaments are partitioned by the dynamic movements of actin fibres to which they are bound. Finally, we showed that partition frequency and filament growth rate in the lamella depend on MLCK, and that MLCK is competing with centrally active ROCK for a limiting pool of monomer with which to drive lamellar filament assembly. Together, our results provide new insights into the mechanism and spatio-temporal regulation of NM2 filament assembly in cells.

SUBMITTER: Beach JR 

PROVIDER: S-EPMC5308804 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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Actin dynamics and competition for myosin monomer govern the sequential amplification of myosin filaments.

Beach Jordan R JR   Bruun Kyle S KS   Shao Lin L   Li Dong D   Swider Zac Z   Remmert Kirsten K   Zhang Yingfan Y   Conti Mary A MA   Adelstein Robert S RS   Rusan Nasser M NM   Betzig Eric E   Hammer John A JA  

Nature cell biology 20170123 2


The cellular mechanisms governing non-muscle myosin II (NM2) filament assembly are largely unknown. Using EGFP-NM2A knock-in fibroblasts and multiple super-resolution imaging modalities, we characterized and quantified the sequential amplification of NM2 filaments within lamellae, wherein filaments emanating from single nucleation events continuously partition, forming filament clusters that populate large-scale actomyosin structures deeper in the cell. Individual partitioning events coincide sp  ...[more]

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