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Activation of Cyclic AMP‐Dependent Protein Kinase in Okadaic Acid‐Treated Neurons Potentiates Neurofilament Fragmentation and Stimulates Phosphorylation of Ser^2^ in the Low‐Molecular‐Mass Neurofilament Subunit by Benoit I. Giasson; James A. Cromlish; Eric S. Athlan; Walter E. Mushynski is a Neuroscience article available to read on EtoBox.

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Abstract: 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 Ser^55^ but had no effect on neurofilament integrity. When PKA was activated in DRG cultures treated with 20–250 n__M__ okadaic acid, neurofilament fragmentation was enhanced, and there was a corresponding increase in phosphorylation of NFL at a novel site. This site was also phosphorylated by PKA in vitro and was determined to be Ser^2^ by mass spectrometric analysis of the purified chymotryptic phosphopeptide. The PKA sites in NFL were dephosphorylated by the purified catalytic subunit of protein phosphatase‐2A but not that of protein phosphatase‐1, and phosphoserine‐2 was a better substrate than phosphoserine‐55. The phosphorylation and dephosphorylation of Ser^2^ and Ser^55^ in NFL may therefore be involved in the modulation of neurofilament dynamics through the antagonistic effects of PKA and protein phosphatase‐2A.

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Author

Benoit I. Giasson; James A. Cromlish; Eric S. Athlan; Walter E. Mushynski

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)

Published

1996

Language

EN

Field

Neuroscience (Life Sciences)