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Title: | Role of receptor protein tyrosine phosphatase α (RPTPα) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels |
Authors: | Imbrici, Paola Tucker, Stephen J. D'Adamo, Maria Cristina Pessia, Mauro |
Keywords: | Potassium channels Phosphorylation Phosphatases Tyrosine |
Issue Date: | 2000 |
Publisher: | Springer |
Citation: | Imbrici, P., Tucker, S. J., D'Adamo, M. C., & Pessia, M. (2000). Role of receptor protein tyrosine phosphatase α (RPTPα) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels. Pflugers Archiv European Journal of Physiology, 441(2-3), 257-262. |
Abstract: | 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 α (RPTPα), 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 RPTPα and specific tyrosine kinases coupled to this receptor. |
URI: | https://www.um.edu.mt/library/oar//handle/123456789/28244 |
Appears in Collections: | Scholarly Works - FacM&SPB |
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