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.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Mol+Biol+Cell
2017 ; 28
(5
): 613-623
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The ultrastructural organization of actin and myosin II filaments in the
contractile ring: new support for an old model of cytokinesis
#MMPMID28057763
Henson JH
; Ditzler CE
; Germain A
; Irwin PM
; Vogt ET
; Yang S
; Wu X
; Shuster CB
Mol Biol Cell
2017[Mar]; 28
(5
): 613-623
PMID28057763
show ga
Despite recent advances in our understanding of the components and spatial
regulation of the contractile ring (CR), the precise ultrastructure of actin and
myosin II within the animal cell CR remains an unanswered question. We used
superresolution light microscopy and platinum replica transmission electron
microscopy (TEM) to determine the structural organization of actin and myosin II
in isolated cortical cytoskeletons prepared from dividing sea urchin embryos.
Three-dimensional structured illumination microscopy indicated that within the
CR, actin and myosin II filaments were organized into tightly packed linear
arrays oriented along the axis of constriction and restricted to a narrow zone
within the furrow. In contrast, myosin II filaments in earlier stages of
cytokinesis were organized into small, discrete, and regularly spaced clusters.
TEM showed that actin within the CR formed a dense and anisotropic array of
elongate, antiparallel filaments, whereas myosin II was organized into laterally
associated, head-to-head filament chains highly reminiscent of mammalian cell
stress fibers. Together these results not only support the canonical
"purse-string" model for contractile ring constriction, but also suggest that the
CR may be derived from foci of myosin II filaments in a manner similar to what
has been demonstrated in fission yeast.
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