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• W4306993428 abstract "In most eukaryotic cells, actin filaments assemble into a shell-like actin cortex under the plasma membrane, controlling cellular morphology, mechanics, and signaling. The actin cortex is highly polymorphic, adopting diverse forms such as the ring-like structures found in podosomes, axonal rings, and immune synapses. The biophysical principles that underlie the formation of actin rings and cortices remain unknown. Using a molecular simulation platform called MEDYAN, we discovered that varying the filament treadmilling rate and myosin concentration induces a finite size phase transition in actomyosin network structures. We found that actomyosin networks condense into clusters at low treadmilling rates or high myosin concentrations but form ring-like or cortex-like structures at high treadmilling rates and low myosin concentrations. This mechanism is supported by our corroborating experiments on live T cells, which exhibit ring-like actin networks upon activation by stimulatory antibody. Upon disruption of filament treadmilling or enhancement of myosin activity, the pre-existing actin rings are disrupted into actin clusters or collapse towards the network center respectively. Our analyses suggest that the ring-like actin structure is a preferred state of low mechanical energy, which is, importantly, only reachable at sufficiently high treadmilling rates." @default.
• W4306993428 created "2022-10-22" @default.
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• W4306993428 date "2022-10-21" @default.
• W4306993428 modified "2023-10-14" @default.
• W4306993428 title "A tug of war between filament treadmilling and myosin induced contractility generates actin rings" @default.
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• W4306993428 doi "https://doi.org/10.7554/elife.82658" @default.
• W4306993428 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36269229" @default.
• W4306993428 hasPublicationYear "2022" @default.
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