To further characterize the morphological changes caused by cytostatic, non-lethal concentrations of mifepristone, the various cancer cell types were cultured in the presence of vehicle or mifepristone for 72 h, and the arrangement of filamentous actin (F-actin) and tubulin filaments contributing to cytoskeletal structure and overall cell morphology were assessed.
Small dark green arrows indicate the bi-directional cortical flow of actin filaments contributing to the construction of the actin ring.
Overall, we demonstrate actin filaments contribute more to elastic stiffness than microtubules but this result is cell type dependent.
Indeed, only a moderate decrease of the production of infectious virions is observed upon microtubule disruption or depolymerization of actin filaments15,24,25,26, suggesting that both the microtubule network and actin filaments contribute jointly to a complex vRNP transport process, and/or that other mechanisms of transport are involved.
Disruption of microtubules or actin filaments leads to a more fluid cytoplasm: both structures, but especially actin filaments, contribute to the elasticity of the intracellular cytoskeleton.
Our results indicate that not only do actin filaments contribute to microscale patterning, but they are the primary determinants of mesoscale silica structural patterning in diatoms.
In contrast, a focus on the properties of semi-dilute gels assumes that intermediate filaments contribute to cell elasticity via entropic mechanisms in which individual filaments and filament bundles are never loaded directly in tension.
Although previous results had demonstrated redistribution of actin in the retrograde direction (i.e., towards the dendritic shaft), it has not been directly shown before that that a vectorial flow of the filaments contributes to such redistribution.
The energy curves in the OT and COT structures indicated that the tensile actin filaments contribute to the major strength of cells, while the compressive microtubules stabilize the cell structure (Figs. 2D and 5).
The mechanism by which the polymerizing actin filaments contribute to membrane invagination is poorly understood.
