By Balch W.E., Channing J.D., Hall A.
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Additional resources for Small GTPases and Their Regulators Part D
5 Direct and indirect evidence suggests that Cs-PI-3,4,5-P3 binds with a modestly higher affinity than Ca-PL4,5-P2. First, whereas 50 /xM Cs-PI-3,4,5-P3 blocks approximately 80% of the binding of radiolabeled C~-PI-3,4,5-P3 ( - 5 /xM) to Vav, 50 ixM Cs-PI-4,5-P2 blocks only 25% of the binding of radiolabeled C~-PI-3,4,5-P3. Second, whereas Cs-PI-3,4,5-P3 stimulates the G E F activity of phosphorylated Vav and Cs-PI-4,5-P2 potently inhibits G E F activity, we found that Vav G E F activity is activated in the presence of equal concentrations of these phosphatidylinositides.
Schuebel, N. Movilla, J. L. Rosa, and X. R. Bustelo. EMBO J. 17, 6608 (1998). 2,) K. Abe, K. L. Rossman, B. Liu, K. D. Ritola, D. Chiang, S. L. Campbell K. Burridge, and C. J. Der, J. Biol. Chem. 275, 10141 (2000). 38 PURIFICATION, MODIFICATION, AND REGULATION  truncation and phosphorylation may relieve intramolecular regulation on GEF activity, it is only partially alleviated in constructs containing other motifs, and thus partially active. This raises the question as to what further signals may be required in vivo for Vav2 to be fully activated?
A) Wild-type and Y174F mutant Hiss,tagged Vav(L) were incubated with baculovirus-produced Lck in the presence of 10 ffM [32p]ATP for 30 min and analyzed by SDS-PAGE and autoradiography. The wild-type but not the Y174F mutant Vav protein was phosphorylated under these conditions, indicating that Y174 is the major site of Lck-dependent phosphorylation of Vav. (B) Quiescent N1H 3T3 cells expressing wild-type Vav, labeled with ortho[32p]phosphate, were stimulated with calf serum. Where indicated, 100 nM wortmannin was added 40 min prior to serum addition.