Studies have mapped 8 tyrosine residues in the cytoplasmic domain of FGFR1 that are important for signaling. Autophosphorylation of residues 653 and 654, located in the activation loop of the kinase, is necessary to maintain the receptor in the active state. Phosphorylation of other tyrosine residues by the intrinsic protein tyrosine kinase activity of the activated receptor creates binding sites on its cytoplasmic tail for membrane bound docking proteins to gather intracellular signaling mediators.
Burgess, WH, Jaye, M, Schlessinger, J, Sorokin, A, Dikic, I, Mohammadi, M
Schlessinger, J, Furdui, CM, Anderson, KS, Lew, ED
Yamazaki, Y, Fukumoto, S, Shimada, T, Iijima, K, Urakawa, I, Okawa, K, Fujita, T, Yameshita, T, Hasegawa, H
Dionne, CA, Jaye, M, Li, N, Schlessinger, J, Honegger, AM, Mohammadi, M, Spivak, T, Li, W
Donoghue, DJ, Hart, KC, Robertson, SC
protein tyrosine kinase activity of FGF23 bound to Klotho and FGFR1c [plasma membrane]
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