Article abstract
Nature Neuroscience 10, 49 - 57 (2007)
Published online: 26 November 2006 | Corrected online: 10 December 2006 | doi:10.1038/nn1810
In the version of this article initially published online, the author affiliations for the first and second authors are incorrect. Both of these authors are at the Massachusetts General Hospital. The error has been corrected for all versions of the article.
PKC-1 regulates secretion of neuropeptides
Derek Sieburth1,2, Jon M Madison1 & Joshua M Kaplan1
Abstract
The secretion of neurotransmitters and neuropeptides is mediated by distinct organelles—synaptic vesicles (SVs) and dense-core vesicles (DCVs), respectively. Relatively little is known about the factors that differentially regulate SV and DCV secretion. Here we show that protein kinase C-1 (PKC-1), which is most similar to the vertebrate PKC 
and 
isoforms, regulates exocytosis of DCVs in Caenorhabditis elegans motor neurons. Mutants lacking PCK-1 activity had delayed paralysis induced by the acetylcholinesterase inhibitor aldicarb, whereas mutants with increased PKC-1 activity had more rapid aldicarb-induced paralysis. Imaging and electrophysiological assays indicated that SV release occurred normally in pkc-1 mutants. By contrast, genetic analysis of aldicarb responses and imaging of fluorescently tagged neuropeptides indicated that mutants lacking PKC-1 had reduced neuropeptide secretion. Similar neuropeptide secretion defects were found in mutants lacking unc-31 (encoding the protein CAPS) or unc-13 (encoding Munc13). These results suggest that PKC-1 selectively regulates DCV release from neurons.
- Department of Molecular Biology, Simches 7, Massachusetts General Hospital, 185 Cambridge St., Boston, Massachusetts 02114, USA.
- Present address: Department of Cell and Neurobiology, Zilkha Neurogenetic Institute, Keck School of Medicine, University of Southern California, Los Angeles, California 90089, USA.
Correspondence to: Joshua M Kaplan1 e-mail: kaplan@molbio.mgh.harvard.edu
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