Evidence for communication between nerve growth factor and protein tyrosine phosphorylation

Néstor Gómez, Nicholas K. Tonks, Christine Morrison, Tony Harmar, Philip Cohen

    Research output: Contribution to journalArticlepeer-review

    94 Citations (Scopus)


    Nerve growth factor (NGF) stimulation of PC12 cells activated two myelin basic protein (MBP) kinase activities > 10-fold within 5 min, which were resolved by chromatography on Mono Q. Each enzyme phosphorylated MBP on threonine and was inactivated by incubation with either CD45, a protein tyrosine phosphatase, or protein phosphatase 2A (PP2A), a serine/threonine phosphatase. The effects of CD45 and PP2A were prevented by vanadate and okadaic acid, respectively. Activation of the MBP-kinases provides a mechanism for communication between NGF and intracellular protein tyrosine phosphorylation.

    Original languageEnglish
    Pages (from-to)119-122
    Number of pages4
    JournalFEBS Letters
    Issue number1-2
    Publication statusPublished - 1 Oct 1990


    • Nerve growth factor
    • Okadaic acid
    • PC12 cell
    • Protein kinase
    • Protein phosphatase
    • Tyrosine phosphorylation

    ASJC Scopus subject areas

    • Structural Biology
    • Biophysics
    • Biochemistry
    • Molecular Biology
    • Genetics
    • Cell Biology


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