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Papers In Press, published online ahead of print May 2, 2003
J. Biol. Chem, 10.1074/jbc.M300492200
Submitted on January 16, 2003
Revised on April 30, 2003
Accepted on May 2, 2003

Ca2+-dependent phosphorylation of syntaxin-1A by DAP-kinase regulates its interaction with Munc-18

Jin-Hua Tian, Sunit Das, and Zu-Hang Sheng

Synaptic Function Unit, NINDS, NIH, Bethesda, Maryland 20892-4154

Corresponding Author: shengz{at}ninds.nih.gov

Syntaxin-1 is a key component of the synaptic vesicle docking/fusion machinery that binds with VAMP/synaptobrevin and SNAP-25 to form the SNARE complex. Modulation of syntaxin binding properties by protein kinases could be critical to the control of neurotransmitter release. Using yeast two-hybrid selection with syntaxin-1A as bait, we have isolated a cDNA encoding the C-terminal domain of DAP-kinase (Death Associated Protein kinase), a calcium/calmodulin-dependent serine/threonine protein kinase. Expression of DAP-kinase in adult rat brain is restricted to particular neuronal subpopulations, including the hippocampus and cerebral cortex. Biochemical studies demonstrate that DAP-kinase binds to and phosphorylates syntaxin-1 at serine-188. This phosphorylation event occurs both in vitro and in vivo in a Ca2+-dependent manner. Syntaxin-1A phosphorylation by DAP-kinase or its S188D mutant, which mimics a state of complete phosphorylation, significantly decreases syntaxin binding to Munc18-1, a syntaxin-binding protein that regulates SNARE complex formation and is required for synaptic vesicle docking. Our results suggest that syntaxin is a DAP-kinase substrate, and provide a novel signal transduction pathway by which syntaxin function could be regulated in response to intracellular [Ca2+] and synaptic activity.


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