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https://doi.org/10.1074/jbc.274.5.2851
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dc.title | RGS16 attenuates Gα(q)-dependent p38 mitogen-activated protein kinase activation by platelet-activating factor | |
dc.contributor.author | Zhang, Y. | |
dc.contributor.author | Neo, S.Y. | |
dc.contributor.author | Han, J. | |
dc.contributor.author | Yaw, L.P. | |
dc.contributor.author | Lin, S.-C. | |
dc.date.accessioned | 2014-12-12T07:34:05Z | |
dc.date.available | 2014-12-12T07:34:05Z | |
dc.date.issued | 1999-01-29 | |
dc.identifier.citation | 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 | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/115916 | |
dc.description.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. | |
dc.description.uri | http://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1074/jbc.274.5.2851 | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.doi | 10.1074/jbc.274.5.2851 | |
dc.description.sourcetitle | Journal of Biological Chemistry | |
dc.description.volume | 274 | |
dc.description.issue | 5 | |
dc.description.page | 2851-2857 | |
dc.description.coden | JBCHA | |
dc.identifier.isiut | 000078319500038 | |
Appears in Collections: | Staff Publications |
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