The protein kinase mos activates MAP kinase kinase in vitro and stimulates the MAP kinase pathway in mammalian somatic cells in vivo

Angel R. Nebreda, Caroline Hill, Nestor Gomez, Philip Cohen, Tim Hunt

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    61 Citations (Scopus)

    Abstract

    The mos protooncogene encodes a serine/threonine protein kinase that is only expressed at significant levels in germ cells. Recombinant malE-mos protein (Xenopus mos protooncogene fused in frame to the maltose binding protein of E. coli) activates MAP kinase in cell-free extracts prepared from Xenopus oocytes and eggs. Here we show that malE-mos immunoprecipitates from Xenopus extracts phosphorylate and activate MAP kinase kinase in vitro, indicating that mos can function as a MAP kinase kinase kinase. Moreover, ectopic expression of mos in mammalian somatic cells, that lack any endogenous mos protein, triggers the activation of MAP kinase in vivo. These results identify the mos protooncogene as a direct activator of the MAP kinase pathway, with the potential to activate this kinase cascade even in cells where normally there is no expression of mos.

    Original languageEnglish
    Pages (from-to)183-187
    Number of pages5
    JournalFEBS Letters
    Volume333
    Issue number1-2
    DOIs
    Publication statusPublished - 25 Oct 1993

    Keywords

    • Elk-1
    • MAP kinase
    • mos
    • Oncogene
    • Protein phosphorylation
    • Signal transduction

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