Journal: The Journal of Biological Chemistry

Article Title: A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors *

doi: 10.1074/jbc.M116.755777

Figure Lengend Snippet: Optimal parameters from the fit. Results are shown for the wild-type FGFR heterodimers and homodimers (A), wild-type and mutant FGFR1·FGFR3 heterodimers (B), wild-type and mutant FGFR2·FGFR3 heterodimers (C), and wild-type and mutant FGFR3 heterodimers and homodimers (D). The left-hand panels display heterodimer stabilities (green bars) alongside homodimer values (8, 31,–33) (white bars) to facilitate comparison. Heterodimer stabilities are calculated from association constants using Equation 3. The right-hand panels show the intrinsic FRET values, with heterodimer results in orange and homodimer values in gray. ANOVA is employed to compare wild-type homodimers and heterodimers (see text for results). Unpaired t tests are performed to determine the significance of the differences between wild-type and mutant heterodimers. *, p < 0.05; **, p < 0.005.

Article Snippet: Finally, K XY and Ẽ were compared using unpaired t tests (the MATLAB function “ttest2”), to determine the effect of the two pathogenic point mutations.

Techniques: Mutagenesis

Journal: The Journal of Biological Chemistry

Article Title: A New Method to Study Heterodimerization of Membrane Proteins and Its Application to Fibroblast Growth Factor Receptors *

doi: 10.1074/jbc.M116.755777

Figure Lengend Snippet: Effects of the achondroplasia and Crouzon syndrome mutations on FGFR heterodimerization Unpaired t tests are performed for the null hypothesis that the wild-type and mutant heterodimers are the same, and the resulting p values are shown. ns indicates that any measured difference is not significant. The largest stabilization effects are observed in wild-type/mutant FGFR3 dimers, and these ΔΔ G values are accompanied by decreases in intrinsic FRET. FGFR1·FGFR3 is slightly stabilized by each mutation and also experiences an increase in intrinsic FRET due to the achondroplasia mutation. The only statistically significant change in FGFR2·FGFR3 caused by the presence of a mutation is a small increase in stability in the presence of the achondroplasia mutation.

Article Snippet: Finally, K XY and Ẽ were compared using unpaired t tests (the MATLAB function “ttest2”), to determine the effect of the two pathogenic point mutations.

Techniques: Mutagenesis