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Fig. 1. NHERF interacts with ßPDGFR in vitro and in vivo in a PDGF-independent manner. (A) Schematic representation of NHERF binding domains. NHERF contains two PSD-95/Dlg/Zo-1 homology (PDZ) domains, protein-protein interaction domains known to associate with specific C-terminal motifs on target proteins. Merlin and ERM (MERM) proteins interact with the 30 amino acids of the C-terminal end of NHERF. (B) Affinity precipitation assays. GST-NHERF fusion proteins encompassing domains PDZ1 (aa 11-97), PDZ1+2 (aa 11-236) and the full-length protein (aa 1-358), affinity precipitate ßPDGFR in glioma 238 cells, whereas PDZ2 alone (aa 149-236) or the C-terminus containing PDZ2 (IC149; aa 149-358), does not. Merlin, but not moesin, is detected in GST-IC149 and full-length NHERF affinity precipitates. (C) The mutant L1106A ßPDGFR does not bind NHERF. Pooled populations of G418-resistant F cells stably expressing the retroviral pLXSN vector (vector), mutant L1106A, wild type (WT) or the kinase-defective mutant K634R, were lysed and assayed for their ability to affinity precipitate with GST-NHERF. (D) Endogenous NHERF immunoprecipitates together with WT but not mutant L1106A ßPDGFR in F cell cultures that were maintained in complete growth medium.





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