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• W79302672 abstract "Research Article15 February 1996free access The heterotrimeric G q protein-coupled angiotensin II receptor activates p21 ras via the tyrosine kinase-Shc-Grb2-Sos pathway in cardiac myocytes. J. Sadoshima J. Sadoshima Cardiovascular Research Center, University of Michigan Medical Center, Ann Arbor 48109-0644, USA. Search for more papers by this author S. Izumo S. Izumo Cardiovascular Research Center, University of Michigan Medical Center, Ann Arbor 48109-0644, USA. Search for more papers by this author J. Sadoshima J. Sadoshima Cardiovascular Research Center, University of Michigan Medical Center, Ann Arbor 48109-0644, USA. Search for more papers by this author S. Izumo S. Izumo Cardiovascular Research Center, University of Michigan Medical Center, Ann Arbor 48109-0644, USA. Search for more papers by this author Author Information J. Sadoshima1 and S. Izumo1 1Cardiovascular Research Center, University of Michigan Medical Center, Ann Arbor 48109-0644, USA. The EMBO Journal (1996)15:775-787https://doi.org/10.1002/j.1460-2075.1996.tb00413.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info p21 ras plays as important role in cell proliferation, transformation and differentiation. Recently, the requirement of p21 ras has been suggested for cellular responses induced by stimulation of heterotrimeric G protein-coupled receptors. However, it remains to be determined how agonists for G protein-coupled receptors activate p21 ras in metazoans. We show here that stimulation of the G q protein-coupled angiotensin II (Ang II) receptor causes activation of p21 ras in cardiac myocytes. The p21 ras activation by Ang II is mediated by an increase in the guanine nucleotide exchange activity, but not by an inhibition of the GTPase-activating protein. Ang II causes rapid tyrosine phosphorylation of Shc and its association with Grb2 and mSos-1, a guanine nucleotide exchange factor of p21 ras. This leads to translocation of mSos-1 to the membrane fraction. Shc associates with the SH3 domain of Fyn whose tyrosine kinase activity is activated by Ang II with a similar time course as that of tyrosine phosphorylation of Shc. Ang II-induced increase in the guanine nucleotide exchange activity was inhibited by a peptide ligand specific to the SH3 domain of the Src family tyrosine kinases. These results suggest that an agonist for a pertussis toxin-insensitive G protein-coupled receptor may initiate the cross-talk with non-receptor-type tyrosine kinases, thereby activating p21 ras using a similar mechanism as receptor tyrosine kinase-induced p21 ras activation. Previous ArticleNext Article Volume 15Issue 41 February 1996In this issue RelatedDetailsLoading ..." @default.
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• W79302672 title "The heterotrimeric G q protein-coupled angiotensin II receptor activates p21 ras via the tyrosine kinase-Shc-Grb2-Sos pathway in cardiac myocytes." @default.
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• W79302672 cites W1558848958 @default.
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• W79302672 cites W1567065545 @default.
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• W79302672 cites W1590871522 @default.
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• W79302672 cites W1810029706 @default.
• W79302672 cites W1849458801 @default.
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• W79302672 cites W2080999736 @default.
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• W79302672 doi "https://doi.org/10.1002/j.1460-2075.1996.tb00413.x" @default.
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