Activation of heterotrimeric G-protein signaling by a ras-related protein. Implications for signal integration |
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Authors: | Cismowski M J Ma C Ribas C Xie X Spruyt M Lizano J S Lanier S M Duzic E |
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Affiliation: | OSI Pharmaceuticals, Tarrytown, New York 10591, the Department of Pharmacology, Medical University of South Carolina, Charleston, South Carolina 29425, USA. mcismowski@neurocrine.com |
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Abstract: | Utilizing a functional screen in the yeast Saccharomyces cerevisiae we identified mammalian proteins that activate heterotrimeric G-protein signaling pathways in a receptor-independent fashion. One of the identified activators, termed AGS1 (for activator of G-protein signaling), is a human Ras-related G-protein that defines a distinct subgroup of the Ras superfamily. Expression of AGS1 in yeast and in mammalian cells results in specific activation of Galpha(i)/Galpha(o) heterotrimeric signaling pathways. In addition, the in vivo and in vitro properties of AGS1 are consistent with it functioning as a direct guanine nucleotide exchange factor for Galpha(i)/Galpha(o). AGS1 thus presents a unique mechanism for signal integration via heterotrimeric G-protein signaling pathways. |
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