Author: ["Martina Schmidt","Sandrine Evellin","Paschal A. Oude Weernink","Frank vom Dorp","Holger Rehmann","Jon W. Lomasney","Karl H. Jakobs"]
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Abstract
Stimulation of phosphoinositide-hydrolysing phospholipase C (PLC) generating inositol-1,4,5-trisphosphate is a major calcium signalling pathway used by a wide variety of membrane receptors, activating distinct PLC-β or PLC-γ isoforms1,2,3,4. Here we report a new PLC and calcium signalling pathway that is triggered by cyclic AMP (cAMP) and mediated by a small GTPase of the Rap family. Activation of the adenylyl cyclase-coupled β2-adrenoceptor expressed in HEK-293 cells or the endogenous receptor for prostaglandin E1 in N1E-115 neuroblastoma cells induced calcium mobilization and PLC stimulation, seemingly caused by cAMP formation, but was independent of protein kinase A (PKA). We provide evidence that these receptor responses are mediated by a Rap GTPase, specifically Rap2B, activated by a guanine-nucleotide-exchange factor (Epac) regulated by cAMP5,6, and involve the recently identified PLC-ɛ isoform7,8,9.Cite this article
Schmidt, M., Evellin, S., Weernink, P. et al. A new phospholipase-C–calcium signalling pathway mediated by cyclic AMP and a Rap GTPase. Nat Cell Biol 3, 1020–1024 (2001). https://doi.org/10.1038/ncb1101-1020 