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The activity of voltage-gated potassium (Kv) channels can be dynamically modulated by several events, including neurotransmitter-stimulated biochemical cascades mediated by G-protein-coupled receptors. By using a heterologous expression system, we show that activating the 5-HT2C receptor inhibits both Kv1.1 and Kv1.2 channels through a tyrosine phosphorylation mechanism. The major molecular determinants of channel inhibition were identified as two tyrosine residues located in the N-terminal region of the Kv channel subunit. Furthermore, we demonstrate that receptor protein tyrosine phosphatase alpha (RPTPalpha), a receptor protein tyrosine phosphatase, co-ordinates the inhibition process mediated via 5-HT2C receptors. We therefore propose that the serotonergic regulation of human Kv1.1 and Kv1.2 channel activity by the 5-HT2C receptor involves the dual coordination of both RPTPalpha and specific tyrosine kinases coupled to this receptor.


Journal article


Pflugers Arch

Publication Date





257 - 262


Animals, Enzyme Inhibitors, Female, Gene Expression, Genistein, Humans, Kinetics, Kv1.1 Potassium Channel, Kv1.2 Potassium Channel, Mutagenesis, Site-Directed, Oocytes, Phosphorylation, Phosphotyrosine, Potassium Channel Blockers, Potassium Channels, Potassium Channels, Voltage-Gated, Protein Tyrosine Phosphatases, Receptor-Like Protein Tyrosine Phosphatases, Class 4, Receptors, Cell Surface, Receptors, Serotonin, Serotonin, Transfection, Vanadates, Xenopus laevis