Phosphorylation of the alpha4 subunit of human alpha4beta2 nicotinic receptors: role of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC).

@article{Pacheco2003PhosphorylationOT,
  title={Phosphorylation of the alpha4 subunit of human alpha4beta2 nicotinic receptors: role of cAMP-dependent protein kinase (PKA) and protein kinase C (PKC).},
  author={Mary A. Pacheco and Tina E. Pastoor and L. v. Wecker},
  journal={Brain research. Molecular brain research},
  year={2003},
  volume={114 1},
  pages={65-72}
}
This study determined whether the alpha4 subunit of human alpha4beta2 neuronal nicotinic receptors is phosphorylated in situ by cyclic AMP-dependent protein kinase (PKA) or protein kinase C (PKC). To accomplish this, human cloned epithelial cells stably transfected with the human alpha4beta2 nicotinic receptor (SH-EP1-halpha4beta2) were incubated with 32P-orthophosphate to label endogenous ATP stores, and the phosphorylation of alpha4 subunits was determined in the absence or presence of PKA or… CONTINUE READING