FGFR3 cysteine mutants Constitutive dimerization of FGFR3 cysteine mutants Activating mutations in FGFR3 that introduce a mutant cysteine residue to the Ig2-Ig3 linker domain or the extracellular juxtamembrane region have been identified in the lethal neonatal disorder thanatophoric dysplasia (Tavormina, 1995a, b; Rousseau, 1996; reviewed in Webster and Donoghue, 1997; Burke, 1998). The presence of the mutant cysteine residue causes ligand-independent dimerization of the receptor through Cys-mediated intramolecular disulphide bonds and leads to increased biological signaling without changing the intrinsic kinase activity of the receptor (d'Avis, 1998; Adar, 2002). More recently, the same mutations, arising somatically, have been identified in a range of cancers including bladder, prostrate and cervical cancer, as well as in multiple myeloma and head and neck squamous cell carcinoma (reviewed in Wesche, 2011). Authored: Rothfels, K, 2012-02-09 Edited: Rothfels, K, 2012-05-16 Pubmed12009017 Pubmed21711248 Pubmed7773297 Pubmed8589699 Pubmed8845844 Pubmed9154000 Pubmed9438390 Pubmed9538690 Reactome Database ID Release 432012084 Reactome, http://www.reactome.org ReactomeREACT_121391 Reviewed: Ezzat, S, 2012-05-15 has a Stoichiometric coefficient of 2 FGFR3 cysteine mutant dimers