S100A8 and gastric cancer: A coimmunoprecipitation experiment and structural modeling of the EPIpYA-B or EPIpYT-B peptide bound to the SH2 domain of PI3K indicated that the threonine (T) residue at the pY + 1 position of EPIpYT-B gives higher affinity to the SH2 domain for binding compared to that of the authentic EPIpYA-B sequence.148 Since clinical evidence shows a weaker association of CagA carrying the EPIYT-B polymorphism with gastric cancer than CagA carrying the EPIYA-B motif, involvement of the EPIYA-B polymorphism-dependent differential activation of PI3K-AKT requires further investigation.148