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|Title:||RGS16 attenuates Gα(q)-dependent p38 mitogen-activated protein kinase activation by platelet-activating factor|
|Source:||Zhang, Y., Neo, S.Y., Han, J., Yaw, L.P., Lin, S.-C. (1999-01-29). RGS16 attenuates Gα(q)-dependent p38 mitogen-activated protein kinase activation by platelet-activating factor. Journal of Biological Chemistry 274 (5) : 2851-2857. ScholarBank@NUS Repository. https://doi.org/10.1074/jbc.274.5.2851|
|Abstract:||The large gene family encoding the regulators of G protein signaling (RGS) proteins has been implicated in the fine tuning of a variety of cellular events in response to G protein-coupled receptor activation. Several studies have shown that the RGS proteins can attenuate G protein-activated extracellular signal-regulated kinase (ERK) group of mitogen-activated protein kinases. We demonstrate herein that the production of inositol trisphosphate and the activation of the p38 group of mitogen-activated protein kinases by the G protein-coupled platelet-activating factor (PAF) receptor was attenuated by RGS16 in both CHO cells transiently and stably expressing RGS16. The inhibition was not observed with RGS2, RGS5, and a functionally defective form of RGS16, RGS16(R169S/F170C). The PAF-induced p38 and ERK pathways appeared to be preferentially regulated by RGS16 and RGS1, respectively. Overexpression of a constitutively active form of Gα11 (Gα11 Q209L) prevented the RGS16-mediated attenuation of p38 activity, suggesting that Gα(q/11) is involved in PAF activation of p38. The Gα(q/11) involvement is further supported by the observation that p38 activation by PAF was pertussis toxin-insensitive. These results demonstrate for the first time that apart from ERK, p38 activation by a G protein-coupled receptor can be attenuated by an RGS protein and provide further evidence for the specificity of RGS function in G protein signaling pathways.|
|Source Title:||Journal of Biological Chemistry|
|Appears in Collections:||Staff Publications|
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