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- W90737823 endingPage "95" @default.
- W90737823 startingPage "59" @default.
- W90737823 abstract "Publisher Summary This chapter discusses the process, regulation, and biological consequence of lipid modification of Ras superfamily small GTPases, with a focus on the role of isoprenoid modification of the Rho and Rab family members. The activity of Ras-related GTPases supports a myriad of physiological and pathophysiological cellular events. Guanine nucleotide binding and hydrolysis regulate Ras-mediated signaling, which governs binding to and activation of downstream effector proteins. However, the subcellular localization of active Ras proteins—and hence the identity of nearby effector and regulatory proteins—can determine the biological outcome of these signaling events. In addition to the diversification of different Ras superfamily GTPase branches by their control by unique regulators and their activation of distinct effectors, their biological roles are further diversified by their posttranslational modification by isoprenoid and fatty acid lipids. Together with other CAAX-signaled and additional posttranslational modifications and (phosphorylation, ubiquitination, SUMOylation), further diversification of the subcellular localization and biological roles of otherwise highly structurally and biochemically related small GTPases can be achieved. These modifications dictate distinct biological functions by impacting the spatiotemporal localization and activity of small GTPases." @default.
- W90737823 created "2016-06-24" @default.
- W90737823 creator A5027303790 @default.
- W90737823 creator A5029996650 @default.
- W90737823 date "2011-01-01" @default.
- W90737823 modified "2023-10-16" @default.
- W90737823 title "Lipid Modification of Ras Superfamily GTPases" @default.
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