Phosphorylation and disruption of intermediate filament proteins in oligodendrocyte precursor cultures treated with calyculin A.

@article{Almazan1993PhosphorylationAD,
  title={Phosphorylation and disruption of intermediate filament proteins in oligodendrocyte precursor cultures treated with calyculin A.},
  author={Guillermina Almazan and Daniel E.H Afar and John C. Bell},
  journal={Journal of neuroscience research},
  year={1993},
  volume={36 2},
  pages={163-72}
}
Treatment of primary cultures of oligodendrocyte precursors with calyculin A, a potent inhibitor of protein phosphatases 1 and 2A, caused the phosphorylation of two intermediate filament components, nestin and vimentin. Phosphoamino acid analysis demonstrated that phosphorylation took place mainly on serine and to a lesser extent on threonine residues. In addition, calyculin A treatment caused a shift in the distribution of the two proteins from the Triton-X-100 insoluble fraction to the… CONTINUE READING