In the skeletal disorder Crouzon syndrome, the FGFR2 mutation (FGFR2C278F) leads to incomplete FGFR2 glycosylation, blocks its membrane localization, and induces the perinuclear accumulation of receptor.97 It was found that FGFR1 and FGFR2 exert their nuclear import through a β-importin-dependent active nuclear pore-mediated mechanisms,93 and proteolytically cleaved FGFR1 and FGFR3 mediated by granzyme B and γ-secretase localize in the nucleus of invading cancer cells and multiple cell lines,94 but the detailed molecular events are still unclear. This evidence concerns the gene FGFR1 and Crouzon syndrome.