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Phospholipase D activation by endogenous 5-hydroxytryptamine 2C receptors is mediated by Galpha13 and pertussis toxin-insensitive Gbetagamma subunits.

Authors: McGrew, L  Chang, MS  Sanders-Bush, E 
Citation: McGrew L, etal., Mol Pharmacol. 2002 Dec;62(6):1339-43.
Pubmed: (View Article at PubMed) PMID:12435801

Phospholipase D activation was measured in primary cultures of rat choroid plexus epithelial cells, which endogenously express the 5-hydroxytryptamine (5-HT) 2C receptor, as well as a heterologous cell line expressing the cloned receptor. In both systems, serotonin stimulation of the 5-HT(2C) receptor activates phospholipase D in addition to phospholipase C, the traditional effector. Specific inhibitors and membrane permeable blocking peptides were used to determine which heterotrimeric G-proteins were involved. Results suggest that both alpha and free betagamma subunits from G(13) heterotrimers are responsible for phospholipase D activation.

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CRRD Object Information
CRRD ID: 1598460
Created: 2006-11-29
Species: All species
Last Modified: 2006-11-29
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.