A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress

Andrew D. Clifton, Peter R. Young, Philip Cohen

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    MAPKAP kinase-2 and MAPKAP kinase-3 mere both activated in response to cellular stress, interleukin-1 and tumour necrosis factor in KB and HeLa cells, and with identical kinetics. Activation of MAPKAP kinase-3, like MAPKAP kinase-2, was prevented by SE 203580, a specific inhibitor of SAPK-2, the upstream activator of MAPKAP kinase-2. MAPKAP kinase-3 and MAPKAP kinase-2 phosphorylated peptide substrates with similar kinetic constants and phosphorylated the same serine residues in HSP27 at the same relative rates. These results establish that MAPKAP kinase-3 lies 'downstream' of SAPK-2 and that it is likely to have overlapping or identical substrates to MAPKAP kinase-2 in vivo.

    Original languageEnglish
    Pages (from-to)209-214
    Number of pages6
    JournalFEBS Letters
    Issue number3
    Publication statusPublished - 2 Sep 1996



    • Cytokine
    • HSP27
    • MAP kinase
    • MAPKAP kinase
    • Stress

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