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

    1433 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

    Fingerprint

    Small Heat-Shock Proteins
    Phosphorylation
    Protein Kinases
    Shock
    Phosphotransferases
    Hot Temperature
    Mitogen-Activated Protein Kinase 3
    Protein Isoforms
    Signal transduction
    Mitogen-Activated Protein Kinase Kinases
    Osmotic Pressure
    Xenopus
    Saccharomyces cerevisiae
    Vertebrates
    Immune Sera
    Signal Transduction
    Fusion reactions
    Cells
    Cell Line
    Enzymes

    Cite this

    Rouse, John ; Cohen, Philip ; Trigon, Sylviane ; Morange, Michel ; Alonso-Llamazares, Ana ; Zamanillo, Daniel ; Hunt, Tim ; Nebreda, Angel R. / A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. In: Cell. 1994 ; Vol. 78, No. 6. pp. 1027-1037.
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    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.",
    author = "John Rouse and Philip Cohen and Sylviane Trigon and Michel Morange and Ana Alonso-Llamazares and Daniel Zamanillo and Tim Hunt and Nebreda, {Angel R.}",
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    A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. / Rouse, John; Cohen, Philip; Trigon, Sylviane; Morange, Michel; Alonso-Llamazares, Ana; Zamanillo, Daniel; Hunt, Tim; Nebreda, Angel R.

    In: Cell, Vol. 78, No. 6, 23.09.1994, p. 1027-1037.

    Research output: Contribution to journalArticle

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    AU - Rouse, John

    AU - Cohen, Philip

    AU - Trigon, Sylviane

    AU - Morange, Michel

    AU - Alonso-Llamazares, Ana

    AU - Zamanillo, Daniel

    AU - Hunt, Tim

    AU - Nebreda, Angel R.

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    AB - 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.

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