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Activation of Extracellular Signal‐Regulated Kinase (ERK) and Akt by Human Serotonin 5‐HT 1B Receptors in Transfected BE(2)‐C Neuroblastoma Cells Is Inhibited by RGS4
Abstract
Abstract: Regulator of G protein signaling (RGS) proteins are GTPase‐activating proteins for heterotrimeric G proteins. One of the best‐studied RGS proteins, RGS4, accelerates the rate of GTP hydrolysis by all G i and G q α subunits yet has been shown to exhibit receptor selectivity. Although RGS4 is expressed primarily in brain, its effect on modulating the activity of serotonergic receptors has not yet been reported. In the present study, transfected BE(2)‐C human neuroblastoma cells expressing human 5‐HT 1B receptors were used to demonstrate that RGS4 can inhibit the coupling of 5‐HT 1B receptors to cellular signals. Serotonin and sumatriptan were found to stimulate activation of extracellular signal‐regulated kinase. This activation was attenuated, but not completely inhibited, by RGS4. Similar inhibition by RGS4 of the protein kinase Akt was also observed. As RGS4 is expressed at high levels in brain, these results suggest that it may play a role in regulating serotonergic pathways.
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Stimulation of serotonin receptors activates the ERK signaling cascade in as little as 5 minutes.
“Stimulation of serotonin receptors activates the ERK signaling cascade in as little as 5 minutes (27–29).”
From An Antidepressant Decreases CSF Aβ Production in Healthy Individuals and in Transgenic AD Mice (2014) · cites this paper as [27]
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Metadata
- Authors
- Lione, A. M., Errico, M., Lin, S. L., & Cowen, D. S.
- Venue
- Journal of Neurochemistry
- Publisher
- Wiley
- Published
- 2000-09
- Volume
- 75
- Issue
- 3
- Pages
- 934-938
- ISSN
- 0022-3042
- 1471-4159
- Cited by
- 73
- References
- 0
- Language
- en
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