Activation of the platelet-derived growth factor receptor-β (PDGFR-β) leads to tyrosine
phosphorylation of the cytoplasmic domain of LRP and alters its association with adaptor
and signaling proteins, such as Shc. The mechanism of the PDGF-induced LRP tyrosine
phosphorylation is not well understood, especially since PDGF not only activates PDGF
receptor but also binds directly to LRP. To gain insight into this mechanism, we used a
chimeric receptor in which the ligand binding domain of the PDGFR-β was replaced with that …