p42 map kinase phosphorylation sites in microtubule-associated protein tau are dephosphorylated by protein phosphatase 2A1 Implications for Alzheimer's disease

Michel Goedert, E. Suzanne Cohen, Ross Jakes, Philip Cohen

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    243 Citations (Scopus)

    Abstract

    The paired helical filament (PHF), which comprises the major fibrous element of the neurofibrillary tangle of Alzheimer's disease, is composed of abnormally phosphorylated microtubule-associated protein tau. Here we show that p42 MAP kinase phosphorylates recombinant tau and converts it to a form which is similar to PHF tau. Of the major serine/threonine protein phosphatases found in mammalian tissues only protein phosphatase 2A (PP2A) could dephosphorylate tau phosphorylated in this manner, with PP2A1 being the most effective form of the enzyme.

    Original languageEnglish
    Pages (from-to)95-99
    Number of pages5
    JournalFEBS Letters
    Volume312
    Issue number1
    DOIs
    Publication statusPublished - 2 Nov 1992

    Keywords

    • Alzheimer's disease
    • Microtubule-associated protein tau
    • Mitogen-activated protein kinase
    • Protein phosphatase 2A

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