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Tyrosine-protein kinase Fer (FER) is a cytoplasmic non-receptor tyrosine kinase of the FPS/FES family, involved in the regulation of signal transduction downstream of several cell surface growth factor receptors including EGFR, PDGFR, and KIT[2][3][5][6]. FER is implicated in the control of actin cytoskeleton organization, cell adhesion, migration, proliferation, and chemotaxis, and has roles in immune responses, mast cell degranulation, leukocyte recruitment, and neuronal signaling[2][3][6][7]. Dysregulation of FER function has been linked to cancer pathogenesis and inflammatory and neurodegenerative processes. It interacts with key molecules such as catenins and focal adhesion kinase, and can phosphorylate substrates including CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1, PTPN11, and potentially STAT3[2][3][5]. FER participates in various signaling pathways that are fundamental in both physiological and pathological cellular processes.
Inhibition of tyrosine kinase activity (by kinase inhibitors such as fostamatinib)[3]
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