Title : Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product.

Pub. Date : 1994 Jan 7

PMID : 8276860






6 Functional Relationships(s)
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1 Previous studies have provided evidence that oncogenic Dbl or an associated protein stimulates GDP dissociation from the human species (Hs) homolog of CDC42. Guanosine Diphosphate MCF.2 cell line derived transforming sequence Homo sapiens
2 We show here that Dbl specifically complexes with the GDP-bound forms of CDC42Hs and RhoA, but not Rac1 or TC10, and that this specificity correlates with the ability of Dbl to act as a GDP-releasing factor. Guanosine Diphosphate MCF.2 cell line derived transforming sequence Homo sapiens
3 We show here that Dbl specifically complexes with the GDP-bound forms of CDC42Hs and RhoA, but not Rac1 or TC10, and that this specificity correlates with the ability of Dbl to act as a GDP-releasing factor. Guanosine Diphosphate MCF.2 cell line derived transforming sequence Homo sapiens
4 Small deletions throughout the Dbl domain, which inactivate transformation, eliminated the ability of Dbl to stimulate GDP dissociation, whereas deletions outside of this domain did not impair either function. Guanosine Diphosphate MCF.2 cell line derived transforming sequence Homo sapiens
5 Small deletions throughout the Dbl domain, which inactivate transformation, eliminated the ability of Dbl to stimulate GDP dissociation, whereas deletions outside of this domain did not impair either function. Guanosine Diphosphate MCF.2 cell line derived transforming sequence Homo sapiens
6 Finally, the Dbl domain itself, when expressed and purified as a recombinant protein, was shown to stimulate GDP dissociation from purified, recombinant CDC42Hs. Guanosine Diphosphate MCF.2 cell line derived transforming sequence Homo sapiens