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Regulatory GTPases

Current Opinion in Structural Biology, 1995
The past year has witnessed a tremendous increase in our understanding of the structures and interactions of the GTPases. The highlights include crystal structures of G alpha subunits, as well as the first complex between a GTPase (Rap1A) and an effector molecule (c-Raf1 Ras-binding domain).
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Chronicles of the GTPase switch

Nature Chemical Biology, 2011
The GTPase switch is a versatile molecular device used by many proteins, such as the small GTPases, to regulate an astounding number of functions. Although the basics of the guanine nucleotide cycle are now well established, the next challenge is to reach an integrated view of how these proteins use it to orchestrate signaling pathways.
Jacqueline Cherfils, Mahel Zeghouf
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Signaling to Rho GTPases

Experimental Cell Research, 1999
Rho GTPases regulate many important processes in all eukaryotic cells, including the organization of the actin cytoskeleton, gene transcription, cell cycle progression, and membrane trafficking. Their activity is regulated by signals originating from different classes of surface receptors including G-protein-coupled receptors, tyrosine kinase receptors,
Lars Kjøller, Alan Hall
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Netrin and the GTPases

Trends in Cell Biology, 2002
Guidance molecules such as the netrins, the semaphorins or ephrins are key regulators of development of the central nervous system. These signals are thought to modulate neurite extension by providing instructive cues that act as attractants or repellents in different cell types.
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RHO–GTPases and cancer

Nature Reviews Cancer, 2002
The RAS oncogenes were identified almost 20 years ago. Since then, we have learnt that they are members of a large family of small GTPases that bind GTP and hydrolyse it to GDP. This is then exchanged for GTP and the cycle is repeated. The switching between these two states regulates a wide range of cellular processes.
Christopher J. Marshall, Erik Sahai
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The Rho GTPases [PDF]

open access: possible, 2005
Rho-family GTPases (p21s) are molecular switches related to the protooncogene Ras: these function in complementary pathways to orchestrate the actin cytoskeleton, regulate cell polarity, microtubule dynamics, membrane transport pathways and modulate a variety of transcriptional events. Rho GTPases are biochemically and structually simple proteins: they
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GTPase Activating Proteins

1993
Since Ras proteins negotiate many signalling pathways leading to cell growth or differentiation, the regulation of Ras activity is vital to cellular health. Ras activity, which derives from a collaboration between Ras and GTP, is terminated by the GTPase activating protein (GAP)-catalyzed hydrolysis of the GTP. Hence, a simple regulatory scheme emerges:
G Bollag, F McCormick
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Effectors for the Rho GTPases

Current Opinion in Cell Biology, 1999
The Rho GTPases are simple enzymes with complex roles in regulating cell morphology, gene transcription, cell cycle progression, apoptosis and tumour progression. The picture has been further complicated by the steady rise in the number of known Rho GTPases as well as in the number of known regulators and target proteins of these GTPases.
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Rho family GTPases

Biochemical Society Transactions, 2012
Rho GTPases comprise a family of molecular switches that control signal transduction pathways in eukaryotic cells. A conformational change induced upon binding GTP promotes an interaction with target (effector) proteins to generate a cellular response. A highly conserved function of Rho GTPases from yeast to humans is to control the actin cytoskeleton,
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Rho GTPases and Cancer

2005
The Rho (Ras-homologous) family of proteins constitutes a major branch of the Ras superfamily of small GTPases, and is evolutionarily conserved across several phyla. Thus far, 25 members have been identified, and these may be divided into 6 subfamilies based on amino acid sequence identity, structural motifs, and biological function.
Pinella Buongiorno, Bharati Bapat
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