Expanded view on the FGFR constructs tested for ciliary localization. (A) Western blot showing expression and maturation of the FGFR2 truncation constructs from Fig. 7, A and B, using 1-day transfection of IMCD3 cells. Actin was used as a loading control. (B) Nucleotide sequence within the region of interest in FGFR constructs used in Fig. 7, D–F. (C) Western blot showing expression and maturation of the FGFR constructs from Fig. 7, D–F, using 1-day transfection of IMCD3 cells. Actin was used as a loading control. (D) Schematic presentation of construct with the L2 motif placed into another location within the juxtamembrane region. (E) Western blot showing expression and maturation of the FGFR2 constructs from Fig. S6 D, using 1-day transfection of IMCD3 cells. Actin was used as a loading control and normalization in densitometry. (F) Ciliary FGFR2 signals were obtained after FGFR2 and ARL13B immunocytochemistry of transfected IMCD3 cells and plotted. (G) Western blot showing the expression of the FGFR2-L424A;R426A variant from Fig. 7 H, using 1-day transfection of IMCD3 cells; actin was used for normalization in densitometry. (H) Nucleotide sequence within the region of interest in FGFR2 constructs used in Fig. 7 J. (I) Western blot showing the expression and maturation of the FGFR constructs from Fig. 7 J, using 1-day transfection of IMCD3 cells. Actin was used as a loading control. Statistical significances were calculated using Welch’s t test (P < 0.05; **P < 0.01, ***P < 0.001); n.s., not significant. Bar plots—mean ± SEM. Box and whiskers—min-max 10–90%. The significance is displayed toward the wild-type FGFR2. The n value indicates the number of independent experiments; the number of analyzed cilia is shown directly in the graph. Source data are available for this figure: SourceData FS6.