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Involvement of protein kinase C-epsilon in activity-dependent potentiation of large dense-core vesicle exocytosis in chromaffin cells SCIE SCOPUS

Title
Involvement of protein kinase C-epsilon in activity-dependent potentiation of large dense-core vesicle exocytosis in chromaffin cells
Authors
Park, YSHur, EMChoi, BHKwak, EJun, DJPark, SJKim, KT
Date Issued
2006-08-30
Publisher
SOC NEUROSCIENCE
Abstract
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)-epsilon is critically involved in ADP. Stimulation of nAChR induced activation of PKC-epsilon, and inhibition of PKC-epsilon by expression of the dominant-negative mutant of PKC-epsilon (DN-PKC-epsilon) or short interfering (siRNA) against PKC-epsilon abolished ADP via decreasing the frequency and quantal size of fused vesicles without affecting basal exocytosis, suggesting that PKC-epsilon is specifically involved in ADP. Electron microscopy revealed that inhibition of PKC-epsilon 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-epsilon, 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-epsilon. Actin filament disassembly induced by MARCKS phosphorylation was also significantly blocked by transfection of DN-PKC-epsilon. 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-epsilon and its downstream target MARCKS via modulating vesicle translocation.
Keywords
LDCV; PKC-epsilon; MARCKS; activity-dependent potentiation; amperometry; neurotransmitter; SUBSTRATE PHOSPHORYLATION; NEUROTRANSMITTER RELEASE; SYNAPTIC PLASTICITY; PHORBOL ESTERS; ACTIVATION; DIACYLGLYCEROL; STIMULATION; TRANSLOCATION; MEMBRANE; ISOFORM
URI
https://oasis.postech.ac.kr/handle/2014.oak/23849
DOI
10.1523/JNEUROSCI.2828-06.2006
ISSN
0270-6474
Article Type
Article
Citation
JOURNAL OF NEUROSCIENCE, vol. 26, no. 35, page. 8999 - 9005, 2006-08-30
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김경태KIM, KYONG TAI
Dept of Life Sciences
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