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Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11945-9.

Phosphorylation of synaptic vesicle proteins: modulation of the alpha SNAP interaction with the core complex.

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1
Howard Hughes Medical Institute, Department of Molecular and Cellular Physiology, Stanford University Medical Center 94305-5428, USA.

Abstract

We analyzed whether synaptic membrane trafficking proteins are substrates for casein kinase II, calcium/calmodulin-dependent protein kinase II, and cAMP-dependent protein kinase (PKA), three kinases implicated in the modulation of synaptic transmission. Each kinase phosphorylates a specific set of the vesicle proteins syntaxin 1A, N-ethylmaleimide-sensitive factor (NSF), vesicle-associated membrane protein (VAMP), synaptosome-associated 25-kDa protein (SNAP-25), n-sec1, alpha soluble NSF attachment protein (alpha SNAP), and synaptotagmin. VAMP is phosphorylated by calcium/calmodulin-dependent protein kinase II on serine 61. alpha SNAP is phosphorylated by PKA; however, the beta SNAP isoform is phosphorylated only 20% as efficiently. alpha SNAP phosphorylated by PKA binds to the core docking and fusion complex 10 times weaker than the dephosphorylated form. These studies provide a first glimpse at regulatory events that may be important in modulating neurotransmitter release during learning and memory.

PMID:
8876242
PMCID:
PMC38163
[Indexed for MEDLINE]
Free PMC Article
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