Journal
SCIENCE
Volume 298, Issue 5600, Pages 2006-2010Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1073776
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- NIDDK NIH HHS [T32-DK07521] Funding Source: Medline
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The Frizzled-2 receptor (Rfz2) from rat binds Wnt proteins and can signal by activating calcium release from intracellular stores. We show that wildtype Rfz2 and a chimeric receptor consisting of the extracellular and transmembrane portions of the beta(2)-adrenergic receptor with cytoplasmic domains of Rfz2 also signaled through modulation of cyclic guanosine 3',5'-monophosphate (cGMP). Activation of either receptor led to a decline in the intracellular concentration of cGMP, a process that was inhibited in cells treated with pertussis toxin, reduced by suppression of the expression of the heterotrimeric GTP-binding protein (G protein) transducin, and suppressed through inhibition of cGMP-specific phosphodiesterase (PDE) activity. Moreover, PDE inhibitors blocked Rfz2-induced calcium transients in zebrafish embryos. Thus, Frizzled-2 appears to couple to PDEs and calcium transients through G proteins.
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