Effect of phosphorylation of Threonine668 and Tyrosine682 on APP, APLP1, and APLP2 to PTB domain containing proteins. (A) Schematic diagrams of the peptides containing PTB domains. (B) The same peptides as in Figure 1 were synthesized. Pull down experiments with immobilized Strep-Tactin resin showed the binding of the peptides to JIP1, JIP2, AIDA-1a, ARH, DAB1, DAB2, ShcC, ShcA, NUMB-p71, NUMB-p72, NUMB-L, X11α, and X11γ. The pull-down samples were analyzed by SDS-PAGE and Comassie-blue staining. (C) Percent binding of the AID, ALID1, ALID2 and the phosphorylated ones to the PTB domain-containing proteins listed above. The interaction that has the greatest binding affinity was designated 100% and the others were represented as a fraction of the maximum binding. All percentages were rounded to the nearest whole number.