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Move Over, Protein Kinase C, You've Got Company: Munc13-1 Is A Novel Diacylglycerol Target That Modulates Neurotransmitter Release

Institutes for Experimental Medicine, and for Biophysical Chemistry, Göttingen/Germany, at the University of Göttingen/Germany, and at the UT Southwestern Medical Center, Dallas/Texas, identified a novel target of the diacylglycerol second messenger pathway that regulates the release of neurotransmitter from nerve cells (Neuron 21, 123-136, July 98).

Information in the brain is transmitted at synapses which are specialized contact zones between a sending and a receiving nerve cell. Upon stimulation, the sending nerve cell releases a substance, the neurotransmitter, which diffuses to the receiving nerve cell where it activates surface receptors. These, in turn, change the physiological state of the receiving cell and thereby transmit the synaptic signal.

Transmitter release at synapses is a complex process that involves a large number of proteins. These regulate the turnover of synaptic vesicles, small membranous intracellular organelles that store neurotransmitter and release it upon stimulation by fusing with the cell membrane. The protein machinery that mediates this release process is subject to regulation by numerous factors. Regulation occurs either directly, e.g. through proteins that interact with the release machinery, or indirectly, e.g. through second messengers that activate protein kinases which in turn modify components of the release apparatus.

One of the most intriguing second messenger pathways in the regulation of neurotransmitter release involves the generation of diacylglycerol, a metabolite of membrane phospholipids. The "textbook" target of the diacylglycerol second messenger pathway is protein kinase C. This kinase enhances transmitter release by phosphorylating proteins of the release machinery and ion channels in the cell membrane. In addition, protein kinase
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Contact: Nils Brose
brose@mail.mpiem.gwdg.de
49-551-3899-725
Max-Planck-Gesellschaft
27-Jul-1998


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