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Journal of Neuroscience, Vol 15, 2385-2395, Copyright © 1995 by Society for Neuroscience
Phosphorylation of rabphilin-3A by Ca2+/calmodulin- and cAMP-dependent protein kinases in vitro
EM Fykse, C Li and TC Sudhof
Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.
Regulation of neurotransmitter release is thought to involve modulation of
the release probability by protein phosphorylation. In order to identify
novel targets for such regulatory processes, we have studied the
phosphorylation of rabphilin-3A in vitro. Rabphilin-3A is a synaptic
vesicle protein that interacts with rab3A in a GTP-dependent manner and
binds Ca2+ in a phospholipid-dependent manner. Here we show that
rabphilin-3A is an efficient substrate for Ca2+/calmodulin- dependent
protein kinase II, which phosphorylates rat rabphilin-3A at residue 234 and
274, and for cAMP-dependent protein kinase, which phosphorylates rat
rabphilin-3A at residue 234. This identifies the middle region of
rabphilin-3A situated between the N-terminal rab3A- binding sequences and
the C-terminal C2-domains involved in Ca2+/phospholipid binding as a
regulatory domain. Thus, rabphilin-3A is a second phosphoprotein on
synaptic vesicles that, similar to synapsin I, may integrate
phosphorylation signals from multiple protein kinase signaling pathways in
the cell.
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