Protein phosphatases and the regulation of mitogen-activated protein kinase signalling

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    The magnitude and duration of signalling through mitogen- and stress-activated kinases are critical determinants of biological effect. This reflects a balance between the activities of upstream activators and a complex regulatory network of protein phosphatases. These mitogen-activated protein kinase phosphatases include both dual-specificity (threonine/tyrosine) and tyrosine-specific enzymes, and recent evidence suggests that a single mitogen-activated protein kinase isoform may be acted upon by both classes of protein phosphatase. In both cases, substrate selectivity is determined by specific protein-protein interactions mediated through noncatalytic amino-terminal mitogen-activated protein kinase binding domains. Future challenges include the determination of exactly how this network of protein phosphatases interacts selectively with mitogen-activated protein kinase signalling complexes to achieve precise regulation of these key pathways in mammalian cells.
    Original languageEnglish
    Pages (from-to)186-92
    Number of pages7
    JournalCurrent Opinion in Cell Biology
    Issue number2
    Publication statusPublished - 1 Apr 2000


    • Biochemistry
    • Cell biology
    • protein phosphatase
    • MAPK
    • MEK
    • Signalling
    • MKP
    • Growth factors


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