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. Author manuscript; available in PMC: 2008 Jun 27.
Published in final edited form as: J Biol Chem. 2004 Apr 19;279(27):28345–28357. doi: 10.1074/jbc.M400457200

Fig. 12. Model for pORF3-mediated ERK activation.

Fig. 12

Binding of ERK to the EB domain of MKP-3 leads to a conformational change in the latter bringing its catalytic domain in close proximity to the phosphothreonine (T-p) and phosphotyrosine (Y-p) residues in activated ERK. This leads to dephosphorylation and inactivation of ERK. The ORF3 protein binds the linker region of MKP-3 (possibly as a dimer) and prevents the conformational change required for its activation following ERK binding to the EB domain. This results in catalytically inefficient MKP-3 and higher levels of active ERK.