Disruption of PDGF Receptor Trafficking by Mutation of Its PI-3 Linase Binding Sites

• DOI: 10.1126/science.8303278
• Publication Date: 2006-10-06T00:01:25Z
• Authors: Marguerite Joly; Andrius Kazlauskas; Fredric S. Fay; Silvia Corvera
• Keywords: Pleckstrin homology domain

Human platelet-derived growth factor receptors (PDGFRs) expressed in human Hep G2 cells internalized and concentrated a juxtanuclear region near the Golgi network within 10 minutes after were treated with PDGF. A PDGFR mutant (F5) that lacks high-affinity binding sites for Src homology 2 domain-containing proteins phosphatidylinositol-3 kinase (PI-3 kinase), Ras guanosine triphosphatase activating protein, phospholipase C-γ, phosphotyrosine phosphatase (Syp) remained at cell periphery. Restoration of PI-3 on F5 completely restored ability receptor to concentrate intracellularly. lacking only failed Thus, appear both necessary sufficient normal endocytic trafficking activated PDGFR.