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KMID : 0613820100200101451
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Journal of Life Science
2010 Volume.20 No. 10 p.1451 ~ p.1457
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Protein Kinase (PKC)-ε Interacts with the Serotonin Transporter (SERT) C-Terminal Region
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Moon Ill-Soo
Seog Dae-Hyun
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Abstract
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Serotonin (5-hydroxytryptamine, 5-HT) is an important mediator of cell-cell signaling in neuronal systems. The serotonin transporter (SERT) on the plasma membrane controls the extracellular 5-HT level by reuptake of released 5-HT from the synaptic cleft, but the underlying regulation mechanism is unclear. Here, we used the yeast two-hybrid system to identify the specific binding protein(s) that interacts with the carboxyl (C)-terminal region of SERT and found a specific interaction with protein kinase C-ε (PKC-ε), a PKC isotype that is characterized as a calcium-independent and phorbol ester/diacylglycerol-sensitive serine/threonine kinase. PKC-ε bound to the tail region of SERT but not to other members of the Na?/Cl- dependent SLC6 gene family in the yeast two-hybrid assay. The C-terminal region of PKC-ε is essential for interaction with SERT. In addition, these proteins showed specific interactions in the glutathione S-transferase (GST) pull-down assay. PKC-ε phosphorylated the peptide of the SERT amino (N)-terminus in vitro. These results suggest that the phosphorylation of SERT by PKC-ε may regulate SERT activity in plasma membrane.
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KEYWORD
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Serotonin, serotonin transporter, PKC-ε, protein-protein interaction, phosphorylation
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