Mechanism of SNARE protein binding and regulation of Cav2 channels by phosphorylation of the synaptic protein interaction site
CT Yokoyama, SJ Myers, J Fu, SM Mockus… - Molecular and Cellular …, 2005 - Elsevier
Cav2. 1 and Cav2. 2 channels conduct P/Q-type and N-type Ca2+ currents that initiate
neurotransmission and bind SNARE proteins through a synaptic protein interaction
(synprint) site. PKC and CaMKII phosphorylate the synprint site and inhibit SNARE protein
binding in vitro. Here we identify two separate microdomains that each bind syntaxin 1A and
SNAP-25 in vitro and are regulated by PKC phosphorylation at serines 774 and 898 and
CaMKII phosphorylation at serines 784 and 896. Activation of PKC resulted in its recruitment …
neurotransmission and bind SNARE proteins through a synaptic protein interaction
(synprint) site. PKC and CaMKII phosphorylate the synprint site and inhibit SNARE protein
binding in vitro. Here we identify two separate microdomains that each bind syntaxin 1A and
SNAP-25 in vitro and are regulated by PKC phosphorylation at serines 774 and 898 and
CaMKII phosphorylation at serines 784 and 896. Activation of PKC resulted in its recruitment …