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

C is involved in numerous biological processes, including cell division and tumorogenesis.

Protein kinase C is activated by a group of tumor-promoting reagents called phorbol esters. These bind to the same site in protein kinase C that interacts with diacylglycerol under physiological conditions. Numerous studies in the past employed phorbol esters as key reagents in the analysis of protein kinase C function, and almost invariably, their effects were attributed to protein kinase C activation. Andrea Betz and Iris Augustin in the laboratory of Nils Brose, head of a research group at the Max Planck Institute for Experimental Medicine, Göttingen/Germany, identified Munc13-1 as a novel brain specific target of phorbol esters whose pharmacological characteristics are almost indistinguishable from those of protein kinase C. In collaboration with Thomas C. Sdhof, University of Texas Southwestern Medical Center, Dallas/Texas, the Göttingen group observed that in living cells, phorbol esters recruit Munc13-1 to the cell membrane and activate it, a feature that so far was thought to be unique to protein kinase C. Together with Michael Rickmann, assistant professor at the University Center for Anatomy, Göttingen/Germany, the researchers were able to show that Munc13-1 is specifically targeted to synaptic transmitter release sites. There it acts as an enhancer of the release process, as U. Ashery and J. Rettig, two electrophysiologists in the group of Erwin Neher at the Max Planck Institute for Biophysical Chemistry, Göttingen/Germany, discovered in an elegant approach. They expressed Munc13-1 in neuromuscular s
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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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