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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

Lione, Angelique M., Errico, Monica, Lin, Stanley L., Cowen, Daniel S.·2000·Journal of Neurochemistry

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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Research works printed but not linked: 23

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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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