Fig. 7: K7 deacetylation of TALDO1 promotes glycolysis in NPC cells independent of enzyme activity. | Cell Death & Disease

Fig. 7: K7 deacetylation of TALDO1 promotes glycolysis in NPC cells independent of enzyme activity.

From: Deacetylation of TALDO1 by HDAC6 promotes glycolysis and nasopharyngeal carcinoma progression through a moonlighting function

Fig. 7

A–C Targeted metabolomics with TALDO1-overexpressing and control SUNE1 cells was performed. A Differentially enriched pathways of SUNE1 cell with overexpressed TALDO1. Differential metabolites were identified based on Log2FC (fold change) ≥1.5, VIP ≥ 1, and FDR-adjusted p < 0.05. VIP values were extracted from the OPLS-DA results. B Altered metabolite levels in the main energy fluxes in TALDO1-overexpressing cells compared to the control cells. C Heatmap of most significant changed metabolites by the targeted metabolomics analysis. The differential metabolites were determined by Log2FC ≥ 1.5 and FDR-adjusted p < 0.05. D, E After transfection with pcDNA3.1-TALDO1 plasmids for 48 h, glucose uptake (D) and lactate production (E) in cell culture medium were measured using the glucose or lactate colorimetric assay kit. F After transfection with Vec, pcDNA3.1-TALDO1(WT), pcDNA3.1-TALDO1(K7R) plasmids into HK1 and SUNE1 cells, the extracellular acidification rate (ECAR) was measured using Seahorse XF assay Kit. The glycolysis and glycolysis capacity were analyzed. G Wild type, K7R, K7Q acetylated mutant recombinant proteins were used to detect TALDO1 enzyme activity in vitro. H Western blot assay was performed to assess the glycolysis rate-limiting enzyme levels in TALDO1 overexpression NPC cells. Data were shown as the mean ± SD of at least three independent experiments. *p < 0.05 and **p < 0.01 and ***p < 0.001.

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