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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Biological Transport
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Cysteine / physiology
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Endocytosis
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Exocytosis
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GTP Phosphohydrolase-Linked Elongation Factors / physiology*
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GTP-Binding Proteins / physiology*
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Guanosine Triphosphate / physiology*
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Humans
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Neurofibromatosis 1 / physiopathology
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Peptide Elongation Factors / physiology
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Peptide Initiation Factors / physiology
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Pheromones / physiology
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Protein Processing, Post-Translational
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Proto-Oncogene Proteins p21(ras) / physiology
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Saccharomyces cerevisiae / physiology
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Signal Transduction*
Substances
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Peptide Elongation Factors
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Peptide Initiation Factors
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Pheromones
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Guanosine Triphosphate
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GTP Phosphohydrolase-Linked Elongation Factors
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GTP-Binding Proteins
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HRAS protein, human
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Proto-Oncogene Proteins p21(ras)
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Cysteine