PTPN3 has been shown to bind to phosphorylated MAPK12 and promote its dephosphorylation, and this interaction is correlated with increased oncogenic signaling through RAS (Hou et al, 2010; Tang et al, 2005; Chen et al, 2014 ). Although the mechanism for this PTPN3 and MAPK12-dependent activation of RAS signaling is not known, dephosphorylation of MAPK12 allows the recovery of larger amounts of MAPK12 from a complex with ERK proteins, suggesting a possible mechanism. A more recent study, however, has found that PTPN3 is itself phosphorylated in a MAPK12-dependent fashion upon binding with phospho-MAPK12. This phosphorylation antagonizes SOB-induced growth inhibition and increases RAS-dependent oncogenic growth (Hou et al, 2012).
Suresh, PS, Chen, G, Mirza, SP, Hou, S, Qi, X, Lepp, A
Chen, G, Qi, X, Mercola, D, Tang, J, Han, J
Wang, AH, Chen, KE, Santhanam, A, Meng, TC, Ho, MR, Chou, CC, Lin, SY, Wu, MJ
Chen, G, Pohl, N, Zhi, HY, Basir, Z, Qi, XM, Li, RS, Loesch, M, Hou, SW
protein serine/threonine kinase activity of PTPN3:p-T183,Y185-MAPK12 [cytosol]
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