Journal
CELLULAR AND MOLECULAR LIFE SCIENCES
Volume 62, Issue 24, Pages 3014-3038Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00018-005-5136-x
Keywords
signal transduction; cancer; GTPase cycle; arginine finger; switch region; cytoskeleton; nuclear transport; protein targeting
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The conversion of guanosine triphosphate (GTP) to guanosine diphosphate (GDP) and inorganic phosphate (P-i) by guanine nucleotide binding proteins (GNBPs) is a fundamental process in living cells and represents an important timer in intracellular signalling and transport processes. While the rate of GNBP-mediated GTP hydrolysis is intrinsically slow, direct interaction with GTPase activating proteins (GAPs) accelerates the reaction by up to five orders of magnitude in vitro. Eighteen years after the discovery of the first GAP, biochemical and structural research has been accumulating evidence that GAPs employ a much wider spectrum of chemical mechanisms than had originally been assumed, in order to regulate the chemical players on the catalytic protein-protein interaction stage.
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