Phosphorylation of microtubule-associated protein tau by isoforms of c-Jun N-terminal kinase (JNK)

Hirotaka Yoshida (Lead / Corresponding author), C. James Hastie, Hilary McLauchlan, Philip Cohen, Michel Goedert

    Research output: Contribution to journalArticlepeer-review

    153 Citations (Scopus)


    Microtubule-associated protein tau in a hyperphosphorylated state is the major component of the filamentous lesions that define a number of neurodegenerative diseases commonly referred to as tauopathies. Hyperphosphorylation of tau at most sites appears to precede filament assembly. Many of the hyperphosphorylated sites are serine/threonine-proline sequences. Here we show that c-Jun N-terminal kinases JNK1, JNK2 and JNK3 phosphorylate tau at many serine/threonine-prolines, as assessed by the generation of the epitopes of phosphorylation-dependent anti-tau antibodies. Of the three protein kinases, JNK2 phosphorylated the most sites in tau, followed by JNK3 and JNK1. Phosphorylation by JNK isoforms resulted in a greatly reduced ability of tau to promote microtubule assembly. These findings extend the number of candidate protein kinases for the hyperphosphorylation of tau in Alzheimer's disease and other neurodegenerative disorders.

    Original languageEnglish
    Pages (from-to)352-358
    Number of pages7
    JournalJournal of Neurochemistry
    Issue number2
    Publication statusPublished - 1 Jul 2004


    • c-Jun N-terminal kinase
    • Stress-activated protein kinase
    • Tau protein
    • Tauopathy

    ASJC Scopus subject areas

    • Biochemistry
    • Cellular and Molecular Neuroscience


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