PathwayStep4203 PathwayStep4204 PathwayStep4205 PathwayStep4206 PathwayStep4202 PathwayStep4201 Autocatalytic phosphorylation of FGFR3 cysteine mutants Constitutive dimerization of FGFR3 cysteine mutants Dimerization of FGFR3 point mutants with enhanced kinase activity Autocatalytic phosphorylation of FGFR3 point mutants with enhanced kinase activity FGFR3c P250R mutant binds to ligand with enhanced affinity Autocatalytic phosphorylation of FGFR3c P250R mutant Signaling by activated point mutants of FGFR3 Activating point mutations in FGFR3 are found in the extracellular ligand-binding domain, the transmembrane region and the tyrosine kinase domain and are believed to result in ligand-independent activation of the receptor (Webster and Donoghue, 1996; Wenbster, 1997). These mutations, although initially characterized in the context of autosomal skeletal disorders, are now being identified in a range of cancers including bladder, cervical, breast, prostate, head and neck, and multiple myeloma (reviewed in Wesche, 2011). Authored: Rothfels, K, 2012-02-09 Edited: Rothfels, K, 2012-05-16 Pubmed21711248 Pubmed8599935 Pubmed8754806 Reactome Database ID Release 431839130 Reactome, http://www.reactome.org ReactomeREACT_121337 Reviewed: Ezzat, S, 2012-05-15