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Munc13-1 Is a Presynaptic Phorbol Ester Receptor that Enhances Neurotransmitter Release

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Ashery,  U.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Neher,  E.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Rettig,  J.
Department of Membrane Biophysics, MPI for biophysical chemistry, Max Planck Society;

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Citation

Betz, A., Ashery, U., Rickmann, M., Augustin, I., Neher, E., Suedhof, T. C., et al. (1998). Munc13-1 Is a Presynaptic Phorbol Ester Receptor that Enhances Neurotransmitter Release. Neuron, 21(1), 123-136. doi:10.1016/S0896-6273(00)80520-6.


Cite as: https://hdl.handle.net/11858/00-001M-0000-0012-FC62-6
Abstract
Munc13-1, a mammalian homolog of C. elegans unc-13p, is thought to be involved in the regulation of synaptic transmission. We now demonstrate that Munc13-1 is a presynaptic high-affinity phorbol ester and diacylglycerol receptor with ligand affinities similar to those of protein kinase C. Munc13-1 associates with the plasma membrane in response to phorbol ester binding and acts as a phorbol ester–dependent enhancer of transmitter release when overexpressed presynaptically in the Xenopus neuromuscular junction. These observations establish Munc13-1 as a novel presynaptic target of the diacylglycerol second messenger pathway that acts in parallel with protein kinase C to regulate neurotransmitter secretion.