Gly369Cys mutation in mouse FGFR3 causes achondroplasia by affecting both chondrogenesis and osteogenesis
J. Clin. Invest. Lin Chen, et al. 104:1517 doi:10.1172/JCI6690 [Go to this article.]

Figure 2
Ligand-independent dimerization and activation of G375C mutant FGFR3. (a) Wild type, G380R, S371C, G375C and K650E mutants of FGFR3 were transiently expressed in 293T cells in the absence or presence of 50 ng/ml aFGF, lysed and immunoprecipitated with anti FGFR3 antibody. Blots were developed using anti-FGFR3 antiserum (upper panel) or anti-phosphotyrosine antibody (lower panel). (b) Receptor phosphotyrosine activity normalized for expression levels of FGFR3. In the absence of aFGF, FGFR3 mutants corresponding to the immunoblot above are phosphorylated. The K650E mutant has the highest basal activity, the G371C mutant is lower in basal activity but still higher than G375C and both are significantly higher than that of the wild type receptor. (c) Wild type and mutant FGFR3 transiently expressed in 293T cells were subjected to chemical cross-linking after being stimulated with 50 ng/ml aFGF. Ligand-independent receptor dimers were found for the S371C and G375C mutants, but not in the wild-type receptor.