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Mol. Cell. Biol., Mar 1997, 1346-1353, Vol 17, No. 3
Copyright © 1997, American Society for Microbiology

Lck regulates Vav activation of members of the Rho family of GTPases

J Han, B Das, W Wei, L Van Aelst, RD Mosteller, R Khosravi-Far, JK Westwick, CJ Der and D Broek
Department of Biochemistry and Molecular Biology, Norris Comprehensive Cancer Center, School of Medicine, University of Southern California, Los Angeles 90033, USA.

Vav is a member of a family of oncogene proteins that share an approximately 250-amino-acid motif called a Dbl homology domain. Paradoxically, Dbl itself and other proteins containing a Dbl domain catalyze GTP-GDP exchange for Rho family proteins, whereas Vav has been reported to catalyze GTP-GDP exchange for Ras proteins. We present Saccharomyces cerevisiae genetic data, in vitro biochemical data, and animal cell biological data indicating that Vav is a guanine nucleotide exchange factor for Rho-related proteins, but in similar genetic and biochemical experiments we fail to find evidence that Vav is a guanine nucleotide exchange factor for Ras. Further, we present data indicating that the Lck kinase activates the guanine nucleotide exchange factor and transforming activity of Vav.


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