Effect of phosphorylation of Thr-668 and Tyr-682 on APP, APLP1, and APLP2 to SH2 domain containing proteins. (A) Schematic diagrams of the structural domains of the various SH2 domain peptides studied. (B) APP C-terminal (AID), APLP1 C-terminal (ALID1), and APLP2 C-terminal (ALID2) and strep-tag control peptides were synthesized. Pull down experiments with immobilized Strep-Tactin resin tested the binding of AID, ALID1, ALID2, and their phosphorylated counterparts to ShcA, ShcB, Grb7, Grb2, Crk, Nck, p85-N, p85-C, Abl, Lyn, Src, SHIP2-N, SHIP2-C, PLCγ-N, and PLCγ-C. 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 SH2 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.