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Nature

Title:		The GTPase superfamily: a conserved switch for diverse cell functions
Author(s):		Bourne HR; Sanders DA; McCormick F;
Address:		"Department of Pharmacology, University of California, San Francisco 94143"
Journal Title:		Nature
Year:		1990
Volume:		348
Issue:		6297
Page Number:		125 - 132
DOI:		10.1038/348125a0
ISSN/ISBN:		0028-0836 (Print) 0028-0836 (Linking)
Abstract:		"Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off' states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch--in bacteria, yeast, flies and vertebrates--suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions"
Keywords:		Animals Biological Transport Cysteine/physiology Endocytosis Exocytosis GTP Phosphohydrolase-Linked Elongation Factors/*physiology GTP-Binding Proteins/*physiology Guanosine Triphosphate/*physiology Humans Neurofibromatosis 1/physiopathology Peptide Elong;
Notes:		"MedlineBourne, H R Sanders, D A McCormick, F eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review England 1990/11/08 Nature. 1990 Nov 8; 348(6297):125-32. doi: 10.1038/348125a0"