Cellular responses regulated by rho-related small GTP-binding proteins
Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 1993Rho-related proteins are members of the ras superfamily of small GTP-binding proteins. Their function in fibroblasts has been analysed using microinjection of living cells. Rho appears to link plasma membrane receptors to the assembly of focal adhesions and actin stress fibres.
Peter Adamson+3 more
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Regulation of macrophage adhesion and migration by Rho GTP‐binding proteins
Journal of Microscopy, 2008SummaryThe Rho family proteins Rac and Rho are believed to be key regulators of cell migration through their effects on the cytoskeleton and cell adhesion. However, recent studies in macrophages indicate that they are not always essential for migration, although they do affect cell shape and adhesion.
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The Role of Prenylated Small GTP-Binding Proteins in the Regulation of Osteoclast Function
Calcified Tissue International, 2003The Ras superfamily of small GTP-binding proteins (also known as small GTPases) comprises more than 80 highly conserved proteins of the Ras, Rho, and Rab subfamilies that are involved in multiple intracellular signalling pathways. These proteins are able to function as molecular switches in the transduction of signals from membrane receptors by cycling
Michael J. Rogers, Fraser P. Coxon
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Regulation of phospholipase D by low molecular weight GTP-binding proteins
Journal of Lipid Mediators and Cell Signalling, 1996Phospholipase D (PLD) is believed to play an important role in cell signal transduction: PLD catalyzes the hydrolysis primarily of phosphatidylcholine (PC) to produce phosphatidic acid that may serve as a lipid second messenger. Although the mechanism of PLD activation has not yet been fully understood, a member of the low molecular weight GTP-binding ...
Yasunori Kanaho+2 more
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The regulation of mitochondrial physiology by organelle‐associated GTP‐binding proteins
Cell Biochemistry and Function, 2002AbstractRecent studies have shown that GTP‐binding proteins can modulate mitochondrial membrane fusion and fission. Furthermore, GTP‐binding proteins can regulate the binding of ribosomes to the mitochondrial membrane and may facilitate the import of proteins through contact points between inner and outer mitochondrial membranes.
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Regulation of the phagocyte respiratory burst by small GTP-binding proteins
Trends in Cell Biology, 1995Bacteria phagocytosed by leukocytes are killed and degraded by toxic oxygen metabolites produced in the phagosome via an NADPH oxidase. NADPH oxidase activity is regulated by small GTP-binding proteins in response to phagocytic stimuli. In this review, Gary Bokoch focuses on the role of Rac in regulating this important phagocytic process.
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Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins
Current Opinion in Cell Biology, 1994Recent progress in our understanding of the regulation of the phagocyte NADPH oxidase by the Rac GTP-binding protein(s) has provided the first detailed glimpse into the mechanisms of leukocyte regulation by a small GTP-binding protein. Studies over the past year have indicated that the activity of the NADPH oxidase can be modulated by regulation of the
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Rab3 Small GTP—Binding Proteins: Regulation by Calcium/Calmodulin
2003Rab proteins, forming a subfamily of 52 predominantly membrane-bound, low molecular weight GTP-binding proteins (G-proteins) of the Ras superfamily, are involved in vesicle traffic between intracellular organelles, endocytosis and exocytosis, and may be regulated by calcium (Ca2 +) and/or calmodulin (CaM).
Richard R. Clough+2 more
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Common Properties of Receptors Coupled to GTP Binding Regulator Proteins
1989A number of membrane receptors coupled to GTP binding regulatory proteins have recently been shown to share structural propertie at the level both of the genes and of the corresponding proteins (Fig. 1 and 2). By comparing results obtained for α2-, β1- and β2-adrenergic catecholamine receptors, M1 to M5 muscarinic acetylcholine receptors as well as ...
C. Delavier+6 more
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Overexpression of developmentally regulated GTP-binding protein-2 increases bone loss
American Journal of Physiology-Endocrinology and Metabolism, 2013The developmentally regulated GTP-binding protein-2 (DRG2) is a novel subclass of GTP-binding proteins. Many functional characteristics of osteoclasts (OC) are associated with small GTPases. We hypothesized that DRG2 affects bone mass via modulating OC activity. Using DRG2 transgenic mice, we investigated the role of DRG2 in bone remodeling.
Hye-Seon Choi+9 more
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