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- W4235072007 abstract "The K-Ras4B GTPase is a major oncoprotein whose signaling activity depends on its correct localization to negatively charged subcellular membranes and nanoclustering in membrane microdomains. Selective localization and clustering are mediated by the polybasic farnesylated C-terminus of K-Ras4B, but the mechanisms and molecular determinants involved are largely unknown. In a combined chemical biological and biophysical approach we investigated the partitioning of semisynthetic fully functional lipidated K-Ras4B proteins [1] into heterogeneous anionic model membranes and membranes composed of viral lipid extracts. Independent of GDP/GTP-loading, K-Ras4B is preferentially localized in liquid-disordered (ld) lipid domains and recruits anionic lipids by an effective, electrostatic lipid sorting mechanism to form new protein-containing fluid domains with higher anionic charge density. In addition, GDP-GTP exchange and, thereby, Ras activation results in a higher concentration of activated K-Ras4B in the nanoscale signaling platforms. Conversely, palmitoylated and farnesylated N-Ras proteins partition into the ld phase and concentrate at the ld/lo phase boundary of heterogeneous membranes [2,3]. Next to the lipid anchor system, the results reveal an involvement of the G-domain in the membrane interaction process by determining minor but yet significant structural reorientations of the GDP/GTP-K-Ras4B proteins at lipid interfaces. A molecular mechanism for isoform-specific Ras signaling from separate membrane microdomains is postulated from the results of this study. 1.) Chen Y-X et al. (2010) Angew. Chem. Int. Ed. 49:6090–6095. 2.) Weise K et al. (2009) J. Am. Chem. Soc. 131:1557–1564. 3.) Vogel A et al. (2009) Angew. Chem. Int. Ed. 48:8784–8787." @default.
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- W4235072007 date "2011-02-01" @default.
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- W4235072007 title "Membrane-Mediated Induction and Sorting of K-Ras Microdomain Signaling Platforms" @default.
- W4235072007 doi "https://doi.org/10.1016/j.bpj.2010.12.689" @default.
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