Journal
CELL
Volume 112, Issue 5, Pages 685-695Publisher
CELL PRESS
DOI: 10.1016/S0092-8674(03)00149-1
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Growth factor receptors activate Ras by recruiting the nucleotide exchange factor son of sevenless (SOS) to the cell membrane, thereby triggering the production of GTP-loaded Ras. Crystallographic analyses of Ras bound to the catalytic module of SOS have led to the unexpected discovery of a highly conserved Ras binding site on SOS that is located distal to the active site and is specific for Ras-GTP. The crystal structures suggest that Ras-GTP stabilizes the active site of SOS allosterically, and we show that Ras-GTP forms ternary complexes with SOScat in solution and increases significantly the rate of SOScat-stimulated nucleotide release from Ras. These results demonstrate the existence of a positive feedback mechanism for the spatial and temporal regulation of Ras.
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