These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Site-specific phosphorylation induces disassembly of vimentin filaments in vitro.
    Author: Inagaki M, Nishi Y, Nishizawa K, Matsuyama M, Sato C.
    Journal: Nature; ; 328(6131):649-52. PubMed ID: 3039376.
    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 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.
    [Abstract] [Full Text] [Related] [New Search]