Abstract
The vimentin network displays remarkable plasticity to support basic cellular functions and reorganizes during cell division. Here, we show that in several cell types vimentin filaments redistribute to the cell cortex during mitosis, forming a robust framework interwoven with cortical actin and affecting its organization. Importantly, the intrinsically disordered tail domain of vimentin is essential for this redistribution, which allows normal mitotic progression. A tailless vimentin mutant forms curly bundles, which remain entangled with dividing chromosomes leading to mitotic catastrophes or asymmetric partitions. Serial deletions of vimentin tail domain gradually impair cortical association and mitosis progression. Disruption of f-actin, but not of microtubules, causes vimentin bundling near the chromosomes. Pathophysiological stimuli, including HIV-protease and lipoxidation, induce similar alterations. Interestingly, full filament formation is dispensable for cortical association, which also occurs in vimentin particles. These results unveil implications of vimentin dynamics in cell division through its interplay with the actin cortex.
Highlights
The vimentin network displays remarkable plasticity to support basic cellular functions and reorganizes during cell division
Insets in f and g display overall projections of merged images. h SW13/cl.2 cells were transfected with red fluorescent protein DsRed Express2 (RFP)//vimentin wt or [1-411] and vimentin distribution in mitosis was observed by immunofluorescence
For direct live network visualization, cells were co-transfected with RFP//vimentin bicistronic plasmids, expressing untagged vimentin, plus a tracer amount of GFPvimentin vectors (Fig. 1b)
Summary
The vimentin network displays remarkable plasticity to support basic cellular functions and reorganizes during cell division. Full filament formation is dispensable for cortical association, which occurs in vimentin particles These results unveil implications of vimentin dynamics in cell division through its interplay with the actin cortex. The vimentin network is highly dynamic and rapidly responds to heat-shock, oxidative and electrophilic stresses, ATP and divalent cation availability, playing a key role in cell adaptation. This fast and versatile remodeling relies on the exchange of subunits or filament segments, as well as on posttranslational modifications. Oxidative and electrophilic modifications of vimentin induce drastic alterations in filament architecture and network reorganization, in which the single cysteine residue plays a crucial role. The vimentin tail has been suggested to undergo conformational changes during filament elongation and assembly in vitro, and to modulate interactions with divalent cations
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