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Next Article 
Journal of Neuroscience, Vol 16, 1965-1974, Copyright © 1996 by Society for Neuroscience
Phosphorylation of brain sodium channels in the I--II linker modulates channel function in Xenopus oocytes
RD Smith and AL Goldin
Department of Microbiology and Molecular Genetics, University of California, Irvine, 92717-4025, USA.
Voltage-gated sodium channels, which initiate action potentials in
mammalian brain neurons, are modulated functionally by cAMP-dependent
protein kinase A (PKA), resulting in reduced sodium current amplitude.
Comparing brain and muscle sodium channels, we show that only the brain
channel is modulated by PKA. The brain sodium channel I-II linker is both
necessary and sufficient for PKA modulation, as shown by exchanging the
I-II linker regions of the two channels. PKA consensus sites in the brain
channel I-II linker were eliminated by deletion and site-specific
mutagenesis. The mutant channels demonstrated decreased levels of
phosphorylation when metabolically labeled in oocytes with [gamma-32P]-ATP,
and they did not respond with a reduction in current magnitude after PKA
induction. Modulation of the brain channel by PKA phosphorylation was
mimicked by adding fixed negative charges at the PKA consensus sites,
suggesting that the decrease in current was a direct result of the negative
charge at one or more of the PKA sites in the I-II linker.
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