Activation of cyclic AMP-dependent protein kinase in okadaic acid-treated neurons potentiates neurofilament fragmentation and stimulates phosphorylation of Ser2 in the low-molecular-mass neurofilament subunit.

@article{Giasson1996ActivationOC,
  title={Activation of cyclic AMP-dependent protein kinase in okadaic acid-treated neurons potentiates neurofilament fragmentation and stimulates phosphorylation of Ser2 in the low-molecular-mass neurofilament subunit.},
  author={Benoit I Giasson and James A. Cromlish and Eric Athlan and Walter E. Mushynski},
  journal={Journal of neurochemistry},
  year={1996},
  volume={66 3},
  pages={1207-13}
}
The activation of cyclic AMP-dependent protein kinase (PKA) in rat dorsal root ganglion (DRG) cultures increased phosphorylation of the low-molecular-mass neurofilament subunit (NFL) at a site previously identified as Ser55 but had no effect on neurofilament integrity. When PKA was activated in DRG cultures treated with 20-250 nM okadaic acid, neurofilament fragmentation was enhanced, and there was a corresponding increase in phosphorylation of NFL at a novel site. This site was also… CONTINUE READING