Abstract
Everywhere we look in biology, GTPases abound. Although the first examples appeared in apparently unrelated contexts — protein synthesis, cancer, hormone action, vision — we now recognize GTPases as members of a large superfamily, encoded by genes apparently descended from a single progenitor. The ability of a primordial GTPase to oscillate between GTP-and GDP-bound conformations furnished an opportunity for evolution to elaborate a diverse and versatile panoply of regulatory switches.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Abo A, Pick E, Hall A, Totty N, Teahan CG, Segal AW (1991) Activation of the NADPH oxidase involves the small GTP-binding protein p21rac1. Nature 353: 668–670
Arshavsky VY, Bownds MD (1992) Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP. Nature 357:416–417
Berstein G, Blank JL, Jhon DY, Exton JH, Rhee SG, Ross EM (1992) Phospholi-pase C-β1 is a GTPase activating protein (GAP) for Gq/11, its physiologic regulator, Cell 70:411–418
Bourne HR (1988) Do GTPases direct membrane traffic in secretion? Cell 53:669–671
Bourne HR, Stryer L (1992) The target set the tempo. Nature 358:541–543
Chant J, Corrado K, Pringle JR, Herskowitz I (1991) Yeast BUD5, encoding a putative GDP-GTP exchange factor, is necessary for bud site selection and interacts with bud formation gene BEM1. Cell 65:1213–1224
Chant J, Herskowitz I (1991) Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway. Cell 65:1203–1212
Clark RA (1990) The human neutrophil respiratory burst oxidase. J Infect Dis 161:1140–1147
Dholakia JN, Wahba AJ (1989) Mechanism of the nucleotide exchange reaction in eukaryotic polypeptide chain initiation. Characterization of the guanine nucleotide exchange factor as a GTP-binding protein. J Biol Chem 264:546–550
Diekmann D, Brill S, Garrett MD, Totty N, Hsuan J, Monfries C, Hall C, Lim L, Hall A (1991) Bcr encodes a GTPase-activating protein for p21rac. Nature 351:400–402
Franke RR, König B, Sakmar TP, Khorana HG, Hofmann KP (1990) Rhodopsin mutants that bind but fail to activate transducin. Science 250:123–125
Knaus UG, Heyworth PG, Evans T, Curnutte JT, Bokoch GM (1991) Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac 2. Science 254:1512–1515
Kroll S, Phillips WJ, Cerione RA (1989) The regulation of the cyclic GMR phosphodiesterase by the GDP-bound form of the a subunit of transducin. J Biol Chem 264:4490–4497
Mizuno T, Kaibuchi K, Ando S, Musha T, Hiraoka K, Takaishi K, Asada M, Nunoi H, Matsuda I, Takai Y (1992) Regulation of the superoxide-generating NADPH oxidase by a small GTP-binding protein and its stimulatory and inhibitory GDP/GTP exchange proteins. J Biol Chem 267:10215–10218
Ridley AJ, Hall A (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389–399
Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401–410
Settleman J, Narasimhan V, Foster LC, Weinberg RA (1992) Molecular cloning of cDNAs encoding the GAP-associated protein p190: implications for a signaling pathway from ras to the nucleus. Cell 69:539–549
Valencia A, Kjeldgaard M, Pai EF, Sander C (1991) GTPase domains of ras p21 oncogene protein and elongation factor Tu: analysis of three-dimensional structures, sequence families, and functional sites. Proc Natl Acad Sci USA 88: 5443–5447
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Bourne, H.R. (1993). GTPases Everywhere!. In: Dickey, B.F., Birnbaumer, L. (eds) GTPases in Biology I. Handbook of Experimental Pharmacology, vol 108 / 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-78267-1_1
Download citation
DOI: https://doi.org/10.1007/978-3-642-78267-1_1
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-78269-5
Online ISBN: 978-3-642-78267-1
eBook Packages: Springer Book Archive