Dominant role of lipid rafts L-type calcium channel in activity-dependent potentiation of large dense-core vesicle exocytosis
SCIE
SCOPUS
- Title
- Dominant role of lipid rafts L-type calcium channel in activity-dependent potentiation of large dense-core vesicle exocytosis
- Authors
- Park, Y; Kim, KT
- Date Issued
- 2009-07
- Publisher
- "WILEY-BLACKWELL PUBLISHING, INC"
- Abstract
- Calcium influx triggers exocytosis by promoting vesicle fusion with the plasma membrane. However, different subtypes of voltage-gated calcium channel (VGCC) have distinct roles in exocytosis. We previously reported that repetitive stimulation induces activity-dependent potentiation (ADP) which represents the increase of neurotransmitter release. Here, we show that L-type VGCC have a dominant role in ADP of large dense-core vesicle (LDCV) exocytosis. Repetitive stimulation activating VGCC can induce ADP, whereas activation of bradykinin (BK) G protein-coupled receptors or purinergic P2X cation channels can not. L-type VGCC has the dominant role in ADP of LDCV exocytosis by regulating Protein Kinase C (PKC)-epsilon translocation and phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS), a target molecule of PKC-epsilon. We provide evidence that L-type VGCC, PKC-epsilon, and MARCKS, but not Q-type VGCC, are selectively located in lipid rafts. Also, PKC-epsilon translocation induced by L-type VGCC activation occurs in lipid rafts. Disruption of lipid rafts abolishes ADP of LDCV exocytosis and changes the fusion pore kinetics without affecting the first stimulation-induced exocytosis, showing that lipid rafts are involved in the potentiation process. Taken together, we suggest that L-type VGCC in lipid rafts selectively mediates ADP of LDCV exocytosis by regulating PKC-epsilon translocation and MARCKS phosphorylation.
- Keywords
- activity-dependent potentiation; amperometry; chromaffin cells; lipid rafts; vesicle; voltage-gated calcium channel; CHROMAFFIN CELLS; MEMBRANE-FUSION; SNARE PROTEINS; CA2+ CHANNELS; PC12 CELLS; SUBTYPES; RELEASE; MARCKS; SITES; SYNAPTOTAGMIN
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/26467
- DOI
- 10.1111/J.1471-4159.2009.06148.X
- ISSN
- 0022-3042
- Article Type
- Article
- Citation
- JOURNAL OF NEUROCHEMISTRY, vol. 110, no. 2, page. 520 - 529, 2009-07
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- There are no files associated with this item.
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