Fig. 1: Site-specific acetylation modulates the catalytic activity of G6PD in cultured mammalian cells.
From: Acetylation-dependent coupling between G6PD activity and apoptotic signaling
a Inhibition of KDACs downregulates G6PD activity. Bars represent the relative Vmax of endogenous G6PD measured in cleared lysates of HEK293T and HCT116 cells cultured in the presence or absence of KDACi. Data were analyzed using one-way ANOVA followed by Tukey’s post hoc test and are presented as mean values ± SD; n = 3 biologically independent samples. b Crystal structure of dimeric human G6PD (PDB ID: 6E08). Putative lysine acetylation sites selected for this study are presented in sticks model. G6P (predicted position) and structural NADP+ are displayed as spheres. The main focus of this study is on residues K89 and K403, which are highlighted in bold. c Acetylation of specific lysine residues is dynamic and differentially regulated by KDACs. Immunoblots show the acetylation level of immunopurified acetylated G6PD-Flag variants, expressed in HEK293T cells cultured in the presence (+) or absence (−) of KDACi. d Site-specific acetylation modulates G6PD activity. Bars represent the relative Vmax of exogenous full-length G6PD measured in cell lysate. Indicated acetylated G6PD variants were expressed in HEK293T (left) and HCT116 (right) cells cultured in the absence (top) or presence (bottom) of KDACi. G6PD activity was normalized to immunoblot intensities of expressed G6PD and displayed relative to AcK414 (pWT G6PD). Data were analyzed using one-way ANOVA followed by Tukey’s post hoc test and are presented as mean values ± SD; n = 4 or 6 (HEK293T), 3, 4, or 5 (HCT116) biologically independent samples. ND, not determined. Source data are provided as a Source Data file.
