Site-specific phosphorylation induces disassembly of vimentin filaments in vitro

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 vimentin. Vimen...

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Bibliographic Details
Published in:Nature (London) 1987-08, Vol.328 (6131), p.649-652
Main Authors: Inagaki, Masaki, Nishi, Yoshimi, Nishizawa, Kimiko, Matsuyama, Mutsushi, Sato, Chikako
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Cattle
Cell structures and functions
Cyclic AMP - pharmacology
cytoskeleton
Cytoskeleton - metabolism
Cytoskeleton, cytoplasm. Intracellular movements
Fundamental and applied biological sciences. Psychology
Intermediate Filaments - metabolism
Magnesium - pharmacology
Magnesium Chloride
Mice
Microscopy, Electron
Molecular and cellular biology
Phosphorylation
Protein Kinase C - metabolism
Protein Kinases - metabolism
Rabbits
vimentin
Vimentin - metabolism
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Summary: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 vimentin. Vimentin exists in a nonphosphorylated as well as in a phosphorylated form, and there is increased phosphorylation of this protein when the filament undergoes marked redistribution in various cells. The role of phosphorylation 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.
ISSN:0028-0836
1476-4687
DOI:10.1038/328649a0