PTPN3 has been shown to bind to phosphorylated MAPK12 and pr...

created [InstanceEdit:8868116] Rothfels, Karen, 2016-04-19
dbId 8868117
displayName PTPN3 has been shown to bind to phosphorylated MAPK12 and pr...
modified [InstanceEdit:9686661] Rothfels, Karen, 2020-05-04
schemaClass Summation
text 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).
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