In summary, protein-protein interactions are the foundation of all signaling events in normal cells as well as in tumor cells. The condensation of the studies displays PTPIP51 as a conductor in the cellular orchestra. We were able to show, that PTPIP51 plays a crucial role in the downstream signaling of the EGFR and the Her2 receptor in Her2 amplified breast cancer cells. Here, PTPIP51 interactions are differentially regulated upon EGFR or Her2 inhibition, providing potential bypass mechanisms. PTPIP51 plays a pivotal role in the Her2 inhibition induced activation of Akt signaling. Furthermore, we highlighted the role of PTPIP51 in the MAPK signaling of Her2 amplified breast cancer cells and found evidence for cross talks towards the NFkappaB signaling. We also firstly described the protein-protein interaction shifts of PTPIP51 induced by the novel small molecule LDC3/Dynarrestin.Nevertheless, the precise mechanisms of several interaction shift and pathway cross talks are still unknown and need extensive further investigation. This study represents a starting point of the functional relevance of PTPIP51 in Her2 amplified breast cancer.
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