Extended Data Fig. 6: Point mutations decreased the palmitoyltransferase activity of the DHHC9-GCP16 complex.
From: Regulation of RAS palmitoyltransferases by accessory proteins and palmitoylation
a,c, Effects of disease-causing mutations R148W and P150S in DHHC9 on the catalytic activity of the DHHC9-GCP16 complex. b,d,e,f,g,h, Effects of point mutations in DHHC9 and GCP16 on the acyltransferase activity of the DHHC9-GCP16 complex. The catalytic activities of the DHHC9-GCP16 complexes were measured using HRAS as the protein substrate and NBD-palmitoyl-CoA as the palmitoyl group donor. The upper panels in (a), (b), (e) and (f) show the SDS-PAGE gels imaged by fluorescence imaging, representing the NBD-palmitoylation levels, while the lower panels show the same gels visualized by Coomassie blue staining. The data in (a), (b), (e) and (f) are the results of a representative experiment from three independent experiments. The data in (c), (d), (g) and (h), which represent the mean ± SD of three independent measurements, were analyzed using the unpaired t-test in Prism to calculate the two-tailed P-values: ****, P < 0.0001; ***, P < 0.001.
