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The Journal of Neuroscience, August 30, 2006, 26(35):8999-9005; doi:10.1523/JNEUROSCI.2828-06.2006

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Cellular/Molecular
Involvement of Protein Kinase C- in Activity-Dependent Potentiation of Large Dense-Core Vesicle Exocytosis in Chromaffin Cells

Yong-Soo Park,¹ Eun-Mi Hur,¹ Bo-Hwa Choi,¹ Eunyee Kwak,¹ Dong-Jae Jun,¹ Su-Jin Park,² and Kyong-Tai Kim¹

¹Department of Life Science, Division of Molecular and Life Sciences, Systems Biodynamics National Core Research Center, Pohang University of Science and Technology, Pohang, 790-784, South Korea, and ²Microscopy and Imaging System, Carl Zeiss Company, Seoul, 121-828, South Korea

Correspondence should be addressed to Dr. Kyong-Tai Kim, Department of Life Science, Pohang University of Science and Technology, San 31, Hyoja Dong, Pohang, 790-784, South Korea. Email: ktk{at}postech.ac.kr

Neurotransmitter release is modulated in an activity-dependent manner. We showed previously that repetitive stimulation of nicotinic acetylcholine receptor (nAChR) induced activity-dependent potentiation (ADP) of large dense-core vesicle (LDCV) exocytosis in chromaffin cells. Here we report that protein kinase C (PKC)- is critically involved in ADP. Stimulation of nAChR induced activation of PKC-, and inhibition of PKC- by expression of the dominant-negative mutant of PKC- (DN-PKC-) or short interfering (siRNA) against PKC- abolished ADP via decreasing the frequency and quantal size of fused vesicles without affecting basal exocytosis, suggesting that PKC- is specifically involved in ADP. Electron microscopy revealed that inhibition of PKC- disrupts activity-induced vesicle translocation required for ADP. We also suggest the involvement of myristoylated alanine-rich C kinase substrate (MARCKS), which is known as a downstream target of PKC-, in ADP of LDCV exocytosis. The level of phospho-MARCKS correlated with the time course of ADP and was reduced by transfection with DN-PKC-. Actin filament disassembly induced by MARCKS phosphorylation was also significantly blocked by transfection of DN-PKC-. Furthermore, knockdown of MARCKS by siRNA resulted in inhibition of ADP and reduction of the number of fused vesicles. Together, we provide evidence that ADP of LDCV exocytosis is regulated by PKC- and its downstream target MARCKS via modulating vesicle translocation.

Key words: LDCV; PKC-; MARCKS; activity-dependent potentiation; amperometry; neurotransmitter

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Received March 10, 2006; revised July 19, 2006; accepted July 20, 2006.

Correspondence should be addressed to Dr. Kyong-Tai Kim, Department of Life Science, Pohang University of Science and Technology, San 31, Hyoja Dong, Pohang, 790-784, South Korea. Email: ktk{at}postech.ac.kr

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