Abstract
Diagnostics and therapies have shown evident advances. Tumour surgery, chemotherapy and radiotherapy are the main techniques in treat cancers. Targeted therapy and drug resistance are the main focus in cancer research, but many molecular intracellular mechanisms remain unknown. Src homology region 2-containing protein tyrosine phosphatase 2 (Shp2) is associated with breast cancer, leukaemia, lung cancer, liver cancer, gastric cancer, laryngeal cancer, oral cancer and other cancer types. Signalling pathways involving Shp2 have also been discovered. Shp2 is related to many diseases. Mutations in the ptpn11 gene cause Noonan syndrome, LEOPARD syndrome and childhood leukaemia. Shp2 is also involved in several cancer-related processes, including cancer cell invasion and metastasis, apoptosis, DNA damage, cell proliferation, cell cycle and drug resistance. Based on the structure and function of Shp2, scientists have investigated specific mechanisms involved in cancer. Shp2 may be a potential therapeutic target because this phosphatase is implicated in many aspects. Furthermore, Shp2 inhibitors have been used in experiments to develop treatment strategies. However, conflicting results related to Shp2 functions have been presented in the literature, and such results should be resolved in future studies.
Highlights
Src homology region 2 (SH2)-containing protein tyrosine phosphatase 2 (Shp2), encoded by the ptpn11gene, is a non-receptor phosphotyrosine phosphatase
Two tandem-arranged SH2 domains are found in the N-terminal region of Shp2 and a phosphatase domain is located in the C-terminal domain of Shp2 [1,2,3]
EphA2 is identified as a tyrosine kinase that phosphorylates Tyr542 and Tyr580 of Shp2 to enhance and prolong extracellular regulated protein kinases (Erk) activation in cells stimulated by growth factors [29]
Summary
Src homology region 2 (SH2)-containing protein tyrosine phosphatase 2 (Shp2), encoded by the ptpn11gene, is a non-receptor phosphotyrosine phosphatase. Previous studies demonstrated that Shp2 is a critical mediator involved in the activation of the small G protein Ras-Erk (Ras-Erk) signalling pathway [25, 26]. EphA2 is identified as a tyrosine kinase that phosphorylates Tyr542 and Tyr580 of Shp2 to enhance and prolong Erk activation in cells stimulated by growth factors [29].
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