Site-specific phosphorylation induces disassembly of vimentin filaments in vitro

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Abstract
Intermediate filaments are a major component of the cytoskeleton of eukaryotic cells. Although there appear to be at least five distinct classes of these filaments, cells of mesenchymal origin and most cells in culture contain the intermediate filament composed of the subunit protein vimentin1. Vimentin exists in a nonphosphorylated as well as in a phosphorylated form1–4, and there is increased phosphorylation of this protein when the filament undergoes marked redistribution in various cells5–8. The role of phosphoryla-tion on assembly–disassembly and organization of the vimentin filament has remained obscure. We report here a stable and purified system allowing biochemical examination of vimentin filament assembly and disassembly. Using this in vitro system, we carried out stoichiometrical phosphorylations, using purified protein kinases. We obtained evidence for site-specific, phosphorylation-dependent disassembly of the vimentin filament.

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