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Published online
doi:10.1083/jcb.200607021
The Journal of Cell Biology, Vol. 176, No. 1, 113-124
The Rockefeller University Press, 0021-9525 $30.00
© Maximov et al.
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Article

Synaptotagmin-12, a synaptic vesicle phosphoprotein that modulates spontaneous neurotransmitter release



Anton Maximov1, Ok-Ho Shin1, Xinran Liu1, and Thomas C. Südhof1,2,3

1 Center for Basic Neuroscience, 2 Department of Molecular Genetics, and 3 Howard Hughes Medical Institute, UT Southwestern Medical Center, Dallas, TX 75390

Correspondence to Thomas C. Südhof: Thomas.Sudhof{at}UTSouthwestern.edu

Central synapses exhibit spontaneous neurotransmitter release that is selectively regulated by cAMP-dependent protein kinase A (PKA). We now show that synaptic vesicles contain synaptotagmin-12, a synaptotagmin isoform that differs from classical synaptotagmins in that it does not bind Ca2+. In synaptic vesicles, synaptotagmin-12 forms a complex with synaptotagmin-1 that prevents synaptotagmin-1 from interacting with SNARE complexes. We demonstrate that synaptotagmin-12 is phosphorylated by cAMP-dependent PKA on serine97, and show that expression of synaptotagmin-12 in neurons increases spontaneous neurotransmitter release by approximately threefold, but has no effect on evoked release. Replacing serine97 by alanine abolishes synaptotagmin-12 phosphorylation and blocks its effect on spontaneous release. Our data suggest that spontaneous synaptic-vesicle exocytosis is selectively modulated by a Ca2+-independent synaptotagmin isoform, synaptotagmin-12, which is controlled by cAMP-dependent phosphorylation.

Abbreviations used in this paper: DIV, days in vitro; IPSC, inhibitory postsynaptic current; mIPSC, mini IPSC; PKA, protein kinase A; VCP, valosin-containing protein.


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