Fig. 1: The enzymatic reaction catalyzed by hSOAT1.

a Chemical structures of the substrates and products of hSOAT1 enzyme are shown. The red dashed line indicates the bond that is broken during acyl-transfer reaction. The hydroxyl group that accepts acyl group is highlighted in red. b The activation effect of cholesterol (CHL) on the esterification reaction of NBD-cholesterol catalyzed by hSOAT1 tetramer and dimer (Data are shown as means ± standard deviations, n = 3 biologically independent samples). c Chemical structure of CI-976 and dose-dependent inhibition curve of hSOAT1 tetramer by CI-976 (The first data point is an artificial point. Data are shown as means ± standard deviations, n = 3 biologically independent samples, and numbers in parentheses are the range for IC50 obtained from curve fitting). d Representative fluorescence-detection size-exclusion chromatography (FSEC) traces of N terminal GFP-tagged SOAT1 dimer at 4 °C (dashed lines) or 45 °C (solid lines) in the presence of 100 µM CI-976 (cyan) or DMSO alone (vehicle, gray). The elution positions of SOAT1 dimer and putative monomer are labeled by arrows. e The peak height ratio of the dimer/monomer in the presence of DMSO alone (vehicle, gray) or 100 µM CI-976 (cyan) (Data are shown as means± standard deviations, n = 3 biologically independent samples, ****p < 0.0001; two-tailed paired t-tests). Source data are provided as a Source Data file.