Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments

@article{Eriksson2004SpecificIV,
  title={Specific in vivo phosphorylation sites determine the assembly dynamics of vimentin intermediate filaments},
  author={John E. Eriksson and Tao He and A V Trejo-Skalli and Ann-Sofi H{\"a}rm{\"a}l{\"a}-Brask{\'e}n and Jukka Hellman and Y H Chou and Robert D. Goldman},
  journal={Journal of Cell Science},
  year={2004},
  volume={117},
  pages={919 - 932}
}
Intermediate filaments (IFs) continuously exchange between a small, depolymerized fraction of IF protein and fully polymerized IFs. To elucidate the possible role of phosphorylation in regulating this equilibrium, we disrupted the exchange of phosphate groups by specific inhibition of dephosphorylation and by specific phosphorylation and site-directed mutagenesis of two of the major in vivo phosphorylation sites determined in this study. Inhibition of type-1 (PP1) and type-2A (PP2A) protein… 
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Identification of phosphorylation-induced changes in vimentin intermediate filaments by site-directed spin labeling and electron paramagnetic resonance.
TLDR
The phosphorylation-induced changes notably affected the proposed "trigger sequences" located in the linker 2 region, which have been hypothesized to mediate the induction of coiled-coil formation and provide further evidence that the linkers play a key role in IF structure and regulation of assembly/disassembly.
Role of phosphorylation on the structural dynamics and function of types III and IV intermediate filaments.
Approaches to study posttranslational regulation of intermediate filament proteins.
Cooperative roles of PAK1 and filamin A in regulation of vimentin assembly and cell extension formation.
Critical Role of Vimentin Phosphorylation at Ser-56 by p21-activated Kinase in Vimentin Cytoskeleton Signaling*
TLDR
The results suggest that vimentin phosphorylation at Ser-56 may inversely regulate PAK activation possibly via the increase in the amount of soluble CAS upon agonist stimulation of smooth muscle cells.
"Heads and tails" of intermediate filament phosphorylation: multiple sites and functional insights.
The Serine/threonine kinase Stk33 exhibits autophosphorylation and phosphorylates the intermediate filament protein Vimentin
TLDR
It is hypothesized that Stk33 is involved in the in vivo dynamics of the intermediate filament cytoskeleton by phosphorylating vimentin.
Vimentin phosphorylation and assembly are regulated by the small GTPase Rab7a
Structural changes in intermediate filament networks alter the activity of insulin‐degrading enzyme
TLDR
It is demonstrated that the nestin‐mediated disassembly of vimentin IFs generates a structure capable of sequestering and modulating the activity of IDE.
Site-specific glycosylation regulates the form and function of the intermediate filament cytoskeleton
TLDR
It is shown that site-specific modification of the prototypical IF protein vimentin with O-linked β-N-acetylglucosamine (O-GlcNAc) mediates its homotypic protein-protein interactions and is required in human cells for IF morphology and cell migration.
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