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. Author manuscript; available in PMC: 2023 Sep 28.
Published in final edited form as: Biochim Biophys Acta Rev Cancer. 2021 Jul 23;1876(2):188595. doi: 10.1016/j.bbcan.2021.188595

Figure 1. FGFR signaling pathway in breast cancer.

Figure 1.

The binding of FGFs to the extracellular domain of FGFR induces dimerization of the receptor and phosphorylation of its intracellular C-terminal domain. The C-terminal phosphorylated tyrosine residues serve as anchors for adaptor proteins that, in turn, activate four distinct signaling cascades: RAS-RAF-MEK-MAPK, PI3K-AKT, JAK-STAT and PLCγ. The activation of these pathways ultimately promotes the expression of transcriptional profiles associated with cell proliferation, differentiation, migration, drug resistance and ERα signaling. TME: tumor microenvironment; HSPG: heparan sulfate proteoglycan; FGFs fibroblast growth factors; FGFR: fibroblast growth factor receptor; PLCγ: phospholipase Cγ; PIP2: phosphatidylinositol-4,5-biphosphate; DAG: diacylglicerol; IP3: inositol triphosphate; PKC: protein kinase C; FRS2α: FGFR substrate 2α; GRB2: growth factor receptor-bound 2; GAB1: GRB2-associated binding protein 1; SOS: son of sevenless; PI3K: phosphatidylinositol-4,5-bisphosphate 3-kinase; JAK: janus activated kinase; STAT: signal transducer and activator of transcription; ERα: estrogen receptor α.