Deletion of the synaptic protein interaction site of the N-type (CaV2.2) calcium channel inhibits secretion in mouse pheochromocytoma cells.

@article{Harkins2004DeletionOT,
  title={Deletion of the synaptic protein interaction site of the N-type (CaV2.2) calcium channel inhibits secretion in mouse pheochromocytoma cells.},
  author={Amy B. Harkins and Anne L. Cahill and James F. Powers and Arthur S. Tischler and Aaron P. Fox},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 42},
  pages={15219-24}
}
Presynaptic N-type Ca2+ channels (CaV2.2, alpha1B) are thought to bind to SNARE (SNAP-25 receptor) complex proteins through a synaptic protein interaction (synprint) site on the intracellular loop between domains II and III of the alpha1B subunit. Whether binding of syntaxin to the N-type Ca2+ channels is required for coupling Ca2+ ion influx to rapid exocytosis has been the subject of considerable investigation. In this study, we deleted the synprint site from a recombinant alpha1B Ca2… CONTINUE READING