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Previous Article | Next Article
Volume 17, Number 18, Issue of September 15, 1997 pp. 6929-6938
Copyright ©1997 Society for NeurosciencePhosphorylation of the Synaptic Protein Interaction Site on N-type Calcium Channels Inhibits Interactions with SNARE Proteins
Received April 28, 1997; revised July 2, 1997; accepted July 7, 1997.
Charles T. Yokoyama2, Zu-Hang Sheng1, and William A. Catterall1 1 Department of Pharmacology and 2 Graduate Program in Neurobiology and Behavior, University of Washington, Seattle, Washington 98195
The synaptic protein interaction (synprint) site on the N-type calcium channel
1B subunit binds to the soluble N-ethylmaleimide-sensitive attachment factor receptor (SNARE) proteins syntaxin and synaptosomal protein of 25 kDa (SNAP-25), and this association may be required for efficient fast synaptic transmission. Protein kinase C (PKC) and calcium and calmodulin-dependent protein kinase type II (CaM KII) phosphorylated a recombinant his-tagged synprint site polypeptide rapidly to a stoichiometry of 3-4 mol of phosphate/mol, whereas cAMP-dependent protein kinase (PKA) and cGMP-dependent protein kinase (PKG) phosphorylated the synprint peptide more slowly to a stoichiometry of <1 mol/mol. Two-dimensional phosphopeptide mapping revealed similar patterns of phosphorylation of synprint polypeptides and native rat brain N-type calcium channel
Key words: N-type calcium channel; synprint site; protein kinase C; Ca2+/CaM kinase II; SNARE complex; syntaxin 1A; SNAP-25
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