Inactivation of jNK ACtivity by mitogen-activated protein kinase phosphatase-2 in Eahy926 endothelial cells is dependent upon agonist-specific jNK translocation to the nucleus

C. Robinson, C.M. Sloss, R.J. Plevin

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28 Citations (Scopus)


We have investigated the termination of agonist-stimulated mitogen-activated protein (MAP) kinase activity in EAhy926 cells by MAP kinase phosphatase-2 (MKP-2). In cells expressing either wild-type (WT) or catalytically inactive (CI)-MKP-2, there was no significant differences in TNFα-stimulated JNK or p38 MAP kinase activity, however hydrogen peroxide (H2O2)-stimulated JNK activity was substantially reduced in WT-MKP-2 expressing clones and enhanced in cells expressing CI-MKP-2. Consistent with these findings, we observed substantial nuclear translocation of JNK occurred in response to H2O2 but not TNFα. Using a phosphospecific anti-JNK antibody, we found that TNFα-stimulated JNK activity was associated principally with the cytosol while in response to H2O2, JNK activity was found within the nucleus. These results show that the role of MKP-2 in terminating JNK activity is determined by the translocation of JNK to the nucleus, which is under agonist-specific regulation and not a universal cellular response to stimulation.
Original languageEnglish
Pages (from-to)29-41
Number of pages13
JournalCellular Signalling
Issue number1
Publication statusPublished - 2001


  • protein kinase
  • endothelial cells
  • translocation

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