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pubmed-article:9438849pubmed:abstractTextThe Son of Sevenless (Sos) proteins control receptor-mediated activation of Ras by catalyzing the exchange of guanosine diphosphate for guanosine triphosphate on Ras. The NH2-terminal region of Sos contains a Dbl homology (DH) domain in tandem with a pleckstrin homology (PH) domain. In COS-1 cells, the DH domain of Sos stimulated guanine nucleotide exchange on Rac but not Cdc42 in vitro and in vivo. The tandem DH-PH domain of Sos (DH-PH-Sos) was defective in Rac activation but regained Rac stimulating activity when it was coexpressed with activated Ras. Ras-mediated activation of DH-PH-Sos did not require activation of mitogen-activated protein kinase but it was dependent on activation of phosphoinositide 3-kinase. These results reveal a potential mechanism for coupling of Ras and Rac signaling pathways.lld:pubmed
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pubmed-article:9438849pubmed:articleTitleCoupling of Ras and Rac guanosine triphosphatases through the Ras exchanger Sos.lld:pubmed
pubmed-article:9438849pubmed:affiliationDepartment of Molecular Genetics and Microbiology, State University of New York at Stony Brook, Stony Brook, NY 11794, USA.lld:pubmed
pubmed-article:9438849pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9438849pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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