1. Rac is required for v-Abl tyrosine kinase to activate mitogenesis
Mark W. Renshaw, Elaine Lea-Chou, Jean Y.J. Wang 
Current Biology 
Volume 6, Issue 1, Pages (January 1996)
DOI: /S (02)

2. Figure 1
Stimulation of pinocytosis by v-Abl. Pinocytosis is revealed by the uptake of lucifer yellow [3]. (a,b) P-3T3 cells, (c,d) A-MuLV transformed P-3T3 cells (AB160 cells), (e,f) D5C3 cells [12] transformed with a temperature-sensitive A-MuLV [21] were incubated with lucifer yellow for 1 h. Pinocytotic activity in P-3T3 and AB160 cells was determined in (a,c) minimal media containing 0.5 % calf serum (CS), or (b,d) after stimulation with 10 % CS. Activity was measured in D5C3 cells in minimal media (e) at 39 °C (restrictive temperature) or (f) at 32 °C (permissive temperature).
Current Biology 1996 6, 76-83DOI: ( /S (02) )

3. Figure 2
Rac N17 blocks DNA synthesis induced by v-Abl. P-3T3 clones stably transfected with a vector expressing Rac N17 under the control of a zinc-inducible promoter (clones 5 and 6), or with the empty vector (clone 1), were infected with A-MuLV. The rate of DNA synthesis was determined by [3H]thymidine incorporation, in media containing 0.5 % CS or 10 % CS, with (filled bars) or without (open bars) zinc, as indicated. Western immunoblotting using an anti-Rac antibody (α-Rac2, shown in lower inserts) demonstrates the expression of the Rac N17 protein in each of the clones. Cells were uninduced (–) or induced (+) with 50μM ZnSO4 for 8 h.
Current Biology 1996 6, 76-83DOI: ( /S (02) )

4. Figure 3
Rac is required for v-Abl to activate ERK2 and JNK1. (a) Activation of ERK2 was determined by coexpression of a hemagglutinin (HA)-epitope-tagged ERK2 (HA–ERK2) [18] with Rac Q61L, v-Ha-Ras, or v-Abl in transient co-transfection assays, as indicated. The effect of dominant-negative mutants Rac N17, Ras N17 or Raf 301 on activation was tested as indicated. ERK2 activity was measured by immune complex in-gel kinase assays with myelin basic protein (p42) as substrate, as described in Materials and methods. The fold-activation shown represents the mean and standard deviation determined from three separate experiments and is normalized to HA–ERK2 protein levels. (b) Stimulation of JNK activity was measured by co-expression of HA–JNK with either v-Abl, Rac Q61L or the control vector, as indicated. The role of Rac in v-Abl activation of JNK was tested by co-expression of Rac N17 as indicated. JNK1 activity was measured by immune complex kinase assays using a glutathione-S-transferase (GST)-tagged amino-terminal Jun fragment as substrate, as described in Materials and methods. The fold-activation shown is of a representative sample and is normalized to HA–JNK1 protein levels.
Current Biology 1996 6, 76-83DOI: ( /S (02) )

5. Figure 3
Rac is required for v-Abl to activate ERK2 and JNK1. (a) Activation of ERK2 was determined by coexpression of a hemagglutinin (HA)-epitope-tagged ERK2 (HA–ERK2) [18] with Rac Q61L, v-Ha-Ras, or v-Abl in transient co-transfection assays, as indicated. The effect of dominant-negative mutants Rac N17, Ras N17 or Raf 301 on activation was tested as indicated. ERK2 activity was measured by immune complex in-gel kinase assays with myelin basic protein (p42) as substrate, as described in Materials and methods. The fold-activation shown represents the mean and standard deviation determined from three separate experiments and is normalized to HA–ERK2 protein levels. (b) Stimulation of JNK activity was measured by co-expression of HA–JNK with either v-Abl, Rac Q61L or the control vector, as indicated. The role of Rac in v-Abl activation of JNK was tested by co-expression of Rac N17 as indicated. JNK1 activity was measured by immune complex kinase assays using a glutathione-S-transferase (GST)-tagged amino-terminal Jun fragment as substrate, as described in Materials and methods. The fold-activation shown is of a representative sample and is normalized to HA–JNK1 protein levels.
Current Biology 1996 6, 76-83DOI: ( /S (02) )