A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins

John Rouse, Philip Cohen, Sylviane Trigon, Michel Morange, Ana Alonso-Llamazares, Daniel Zamanillo, Tim Hunt, Angel R. Nebreda

    Research output: Contribution to journalArticle

    1443 Citations (Scopus)

    Abstract

    MAPK-activated protein kinase-2 (MAPKAP kinase-2) is activated in vitro by the p42 and p44 isoforms of MAPK (p42p44MAPK). In several cell lines, however, MAPKAP kinase-2 is activated by sodium arsenite, heat shock, or osmotic stress and not by agonists that activate p42p44MAPK. We have identified a MAPK-like enzyme that acts as a MAPKAP kinase-2 reactivating kinase (RK). RK is recognized by an antiserum raised against a Xenopus MAPK (Mpk2), which is most similar to HOG1 from S. cerevisiae. We also identified a RK kinase (RKK) on the basis of its ability to activate either RK or a GST-Mpk2 fusion protein. The RKK, RK, and MAPKAP kinase-2 constitute a new stress-activated signal transduction pathway in vertebrates that is distinct from the classical MAPK cascade.
    Original languageEnglish
    Pages (from-to)1027-1037
    Number of pages11
    JournalCell
    Volume78
    Issue number6
    DOIs
    Publication statusPublished - 23 Sep 1994

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