The Gbetagamma dimer drives the interaction of heterotrimeric Gi proteins with nonlamellar membrane structures

The Journal of Biological Chemistry
Oliver VöglerPablo V Escribá

Abstract

Heterotrimeric G proteins are peripheral membrane proteins that propagate signals from membrane receptors to regulatory proteins localized in distinct cellular compartments. To facilitate signal amplification, G proteins are in molar excess with respect to G protein-coupled receptors. Because G proteins are capable of translocating from membrane to cytosol, protein-lipid interactions play a crucial role in signal transduction. Here, we studied the binding of heterotrimeric G proteins (Galphabetagamma) to model membranes (liposomes) and that of the entities formed upon receptor-mediated activation (Galpha and Gbetagamma). The model membranes used were composed of defined membrane lipids capable of organizing into either lamellar or nonlamellar (hexagonal H(II)) membrane structures. We demonstrated that although heterotrimeric G(i) proteins and Gbetagamma dimers can bind to lipid bilayers of phosphatidylcholine, their binding to membranes was markedly and significantly enhanced by the presence of nonlamellar phases of phosphatidylethanolamine. Conversely, activated G protein alpha subunits showed an opposite membrane binding behavior with a marked preference for lamellar membranes. These results have important consequences in cel...Continue Reading

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Citations

Sep 3, 2011·The Journal of Physical Chemistry. B·Javier CerezoJosé Pedro Cerón-Carrasco
Sep 6, 2008·Proceedings of the National Academy of Sciences of the United States of America·S TerésP V Escribá
May 16, 2012·Proceedings of the National Academy of Sciences of the United States of America·Silvia TerésPablo V Escribá
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Oct 28, 2006·Biochimica Et Biophysica Acta·Pablo V EscribáOliver Vögler
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Apr 12, 2008·Biochimica Et Biophysica Acta·Oliver VöglerPablo V Escribá

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