[HTML][HTML] Ca2+-dependent phosphorylation of syntaxin-1A by the death-associated protein (DAP) kinase regulates its interaction with Munc18
JH Tian, S Das, ZH Sheng - Journal of Biological Chemistry, 2003 - ASBMB
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 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 death-associated protein (DAP) kinase, a
calcium/calmodulin-dependent serine/threonine protein kinase. Expression of DAP kinase in …
with VAMP/synaptobrevin and SNAP-25 to form the SNARE complex. Modulation of syntaxin
binding properties by protein kinases could be critical to 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 death-associated protein (DAP) kinase, a
calcium/calmodulin-dependent serine/threonine protein kinase. Expression of DAP kinase in …