Constitutive dimerization of FGFR4 Y367C mutant Authored: Rothfels, K, 2012-02-09 Edited: Rothfels, K, 2012-05-16 Pubmed18056464 Pubmed19946327 Pubmed8696350 Pubmed8845844 Pubmed9438390 Reactome Database ID Release 432012086 Reactome, http://www.reactome.org ReactomeREACT_120721 Reviewed: Ezzat, S, 2012-05-15 The Y367C mutation in FGFR4 was identified in a breast cancer cell line in a cDNA screen of kinase mutants (Ruhe, 2007). This residue is paralogous to the FGFR2 Y375C and FGFR3 Y373C mutations that have been shown to result in increased receptor activation (Prezylepa, 1996; Rousseau, 1996; d'Avis, 1998). Biochemical characterization of the FGFR4 Y367C mutation revealed that it undergoes spontaneous dimerization independent of ligand stimulation, presumably mediated by the aberrant cysteine residues in the extracellular region of the receptor (Roidl, 2009), thus affecting FGFR4 activity without directly altering its kinase activity. has a Stoichiometric coefficient of 2 FGFR4 Y367C mutant dimer