Fig. 6: DHHC9 expression positively correlates with GLUT1 PM localization in GBM specimens and indicates clinical aggressiveness of GBM.

a, b Sixty-eight human primary GBM specimens were immunohistochemically stained with indicated antibodies. Representative photos of tumors are shown (a). Immunohistochemistry staining scores of DHHC9 and PM-localized GLUT1 were analyzed by the two-tailed Pearson correlation (b). Note that some of the dots on the graphs represent more than one specimen (i.e., some scores overlapped). c Kaplan–Meier method was used to plot survival curves in human GBM specimens (n = 68) with high (5–8 staining scores, red curve) and low (0–4 staining scores, blue curve) levels of DHHC9 and PM-localized GLUT1. The two-tailed log-rank test was used to compare the overall survival rate. Empty circles represent censored data from patients alive at the last clinical follow-up. d A mechanism of S-palmitoylated GLUT1-dependent glycolysis. GLUT1 Cys207 palmitoylation catalyzed by DHHC9 resulted in PM localization of GLUT1, leading to enhanced uptake of glucose, thereby promoting glycolysis, cell growth, and GBM tumorigenesis. P values were calculated by the two-tailed Pearson correlation (b) and the two-tailed log-rank test (c). Scale bar, 20 μm (a). Source data are provided as a Source Data file.