title: The GTPase superfamily: a conserved switch for diverse cell functions.
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.
authors.affiliation: Department of Pharmacology, University of California, San Francisco 94143.
authors.forename: H R
authors.initials: HR
authors.lastname: Bourne
authors.forename: D A
authors.initials: DA
authors.lastname: Sanders
authors.forename: F
authors.initials: F
authors.lastname: McCormick
mesh_terms: D000818:Animals; D001692:Biological Transport; D003545:Cysteine / Q000502:physiology; D004705:Endocytosis; D005089:Exocytosis; D020963:GTP Phosphohydrolase-Linked Elongation Factors / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000502:physiology*; D006160:Guanosine Triphosphate / Q000502:physiology*; D006801:Humans; D009456:Neurofibromatosis 1 / Q000503:physiopathology; D010445:Peptide Elongation Factors / Q000502:physiology; D010448:Peptide Initiation Factors / Q000502:physiology; D010675:Pheromones / Q000502:physiology; D011499:Protein Processing, Post-Translational; D016283:Proto-Oncogene Proteins p21(ras) / Q000502:physiology; D012441:Saccharomyces cerevisiae / Q000502:physiology; D015398:Signal Transduction
chemical_list: D010445:Peptide Elongation Factors; D010448:Peptide Initiation Factors; D010675:Pheromones; D006160:Guanosine Triphosphate; D020963:GTP Phosphohydrolase-Linked Elongation Factors; D019204:GTP-Binding Proteins; C501009:HRAS protein, human; D016283:Proto-Oncogene Proteins p21(ras); D003545:Cysteine