Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766.
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Sorokin A, Mohammadi M, Huang J, Schlessinger J
Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766.
J Biol Chem. 1994 Jun 24;269(25):17056-61.
- PubMed ID
- 7516330 [ View in PubMed]
- Abstract
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.