ABL1 and cancer: Another possible CagA target that mediates morphological changes and motility is c-Abl, a nonreceptor tyrosine kinase that interacts with CagA and plays a role in CagA phosphorylation.[8, 9] Evidence shows that Src regulates c-Abl activity, which is activated in response to integrin-mediated CagA translocation.[8, 9, 35, 36] Additionally, c-Abl has been shown in recent years to influence cancer invasion and anchorage independence, although the exact mechanism is still unknown.[37–39] Therefore, CagA association with c-Abl may promote cell motility.