Fig. 6: The activation of the PI3Kα-Akt pathway by Vav2 is F-actin-dependent and Pak family-independent.
From: Vav2 catalysis-dependent pathways contribute to skeletal muscle growth and metabolic homeostasis
a, b Representative images of the subcellular localization of the bioreporter mCherry-Akt PH in starved C2C12 cells expressing the indicated EGFP-tagged proteins (top) and treated with the actin-depolymerizing drugs shown on top. The quantification of membrane-translocated mCherry-Akt PH (red) and GFP-protein (green) are shown at the bottom. Values are represented as mean ± SEM. **, P = 0.0015; ***, P = 0.0007 (cytochalasin D-treated, Rac1Q61L-transfected cells), and P < 0.000001 (rest of analyses) relative to untreated cells transfected with an empty vector using two-way ANOVA and Holm–Sidak’s multiple comparison tests (n = 3 independent experiments). Scale bar, 10 μm. c Signaling properties of the indicated Rac1 switch mutant proteins. +, activation; −, lack of activation. d Representative image showing the subcellular localization of mCherry-Akt PH in starved, nonstimulated C2C12 cells transiently transfected with the indicated EGFPs (top). Data are shown as in a. ***, P = 0.00004 (EGFP) and P = 0.000003 (PH-Akt) relative to cells expressing Rac1Q61L using a Kruskal–Wallis test and two-sided Dunn’s multiple comparison tests (n = 3 independent experiments). Scale bar, 10 μm. e Schematic representation of the Vav2-Rac1 signaling pathway in muscle cells according to the data obtained in Figs. 4–6. Source data for this figure are provided as a Source data file.
