Overexpressed FGFR2 Dimerization of overexpressed FGFR2 Authored: Rothfels, K, 2012-02-09 Edited: Rothfels, K, 2012-05-16 Overexpressed FGFR2 in gastric and breast cancer cells has been shown to undergo ligand-independent dimerization (Takeda, 2007; Kunii, 2008; Moffa, 2004; Turner, 2010). Full-length FGFR2 is weakly transforming in NIH 3T3 cells, and is thought to possess a transformation-inhibiting domain in the C-terminus (Itoh, 1994). Interestingly, many cancers with amplifications of FGFR2 show preferrential expression of C-terminally truncated FGFR2 variants, designated C2 and C3, with 788 or 769 residues instead of the wild-type 822 (Hattori, 1990; Itoh, 1994; Ueda, 1999). These variants, which lack a number of carboxy-terminal tyrosine residues, show increased transforming potency compared to the full-length receptor (Cha, 2008; Cha, 2009), and have been shown to be constitutively active and to dimerize spontaneously (Takeda, 2007). Pubmed10626794 Pubmed15561780 Pubmed17505008 Pubmed18337450 Pubmed18381441 Pubmed19103595 Pubmed20101236 Pubmed2377625 Pubmed8205545 Reactome Database ID Release 432029988 Reactome, http://www.reactome.org ReactomeREACT_121115 Reviewed: Ezzat, S, 2012-05-15 has a Stoichiometric coefficient of 2 Overexpressed FGFR2 homodimers