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pubmed-article:1756860pubmed:abstractTextTo determine the amino acid residues required for the signal-transducing activity of the human c-Ha-Ras protein, we introduced point mutations at residues 45-54 near the 'effector region' (residues 32-40). We transfected PC12 cells with these mutant genes and also micro-injected the mutant proteins, bound with an unhydrolyzable GTP analog, into PC12 cells. Both procedures showed that Val45----Glu and Gly48----Cys mutations impaired the ability of the Ras protein to induce morphological change of PC12 cells. These mutations did not affect the guanine nucleotide-binding activity or GTPase activity in the absence or presence of bovine GTPase-activating protein (GAP). Therefore, the Val45 and Gly48 residues should be included by definition in the effector region responsible for the signal transduction, while only a subset of the effector-region residues is required for enhancement of the GTPase activity by GAP.lld:pubmed
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pubmed-article:1756860pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:1756860pubmed:articleTitleIdentification of amino acid residues of Ras protein that are essential for signal-transducing activity but not for enhancement of GTPase activity by GAP.lld:pubmed
pubmed-article:1756860pubmed:affiliationDepartment of Biophysics and Biochemistry, Faculty of Science, University of Tokyo, Japan.lld:pubmed
pubmed-article:1756860pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1756860pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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