Abstract
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 cycle between two conformational states, with the GTP-bound form regarded as active, while the GDP-bound state is essentially inactive. Conversion between these states is brought about by hydrolysis of bound GTP. The GTPases in their active form can recognize a variety of target proteins and thereby generate a response until GTP hydrolysis returns the switch to an ‘off’ state. The Rho family of GTPases is now intensively studied by cell biologists, as its members have turned out to be key regulators of many aspects of cell behaviour. In this introductory chapter I discuss how Rho proteins become activated by GEFs in response to extracellular signals, and in particular how integrin signaling might impinge on Rhos. At this stage our knowledge of many of these pathways is rudimentary, thus much still needs to be done to uncover specific pathways that regulate of Rho proteins in vivo. This volume covers what is known of Rho proteins in vertebrate systems with some reference to lower model organisms. The molecular and structural data is covered in some depth; in this ‘post genomic’ era we are also able to provide a panoramic view of the various protein families that have emerged as key players in Rho GTPases signaling.
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Manser, E. (2005). The Rho GTPases. In: Manser, E. (eds) RHO Family GTPases. Proteins and Cell Regulation, vol 3. Springer, Dordrecht. https://doi.org/10.1007/1-4020-3462-8_1
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