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J Biol Chem. 1994 Jun 24;269(25):17056-61.

Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766.

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Department of Pharmacology, New York University Medical Center, New York 10016.


Binding of fibroblast growth factor (FGF) to the fibroblast growth factor receptor leads to autophosphorylation of the receptor on several tyrosine residues. Wild-type FGF receptor 1 (flg) and a mutated receptor (Y766F), in which an autophosphorylation site (Tyr-766) was mutated to phenylalanine, were expressed in rat myoblasts and in hematopoietic Ba/F3 cells. It was found that the point mutation at Tyr-766 resulted in a decrease in FGF receptor internalization, as well as a reduction in both ligand-induced FGF receptor down-regulation and degradation. It has been shown previously that phosphorylation of Tyr-766 is essential for interaction with phospholipase C gamma and that the Y766F FGF receptor mutant is unable to stimulate phosphatidylinositol hydrolysis and Ca2+ release from internal stores. The results presented in this report indicate that Tyr-766 is also essential for cellular trafficking of FGF receptor.

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