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Millward, T.A., Zolnierowicz, S., Hemmings, B.A. (1999). Regulation of protein kinase cascades by protein phosphatase 2A.  Trends Biochem. Sci. 24(5): 186--191.
FlyBase ID
FBrf0108474
Publication Type
Review
Abstract

Many protein kinases themselves are regulated by reversible phosphorylation. Upon cell stimulation, specific kinases are transiently phosphorylated and activated. Several of these protein kinases are substrates for protein phosphatase 2A (PP2A), and PP2A appears to be the major kinase phosphatase in eukaryotic cells that downregulates activated protein kinases. This idea is substantiated by the observation that some viral proteins and naturally occurring toxins target PP2A and modulate its activity. There is increasing evidence that PP2A activity is regulated by extracellular signals and during the cell cycle. Thus, PP2A is likely to play an important role in determining the activation kinetics of protein kinase cascades.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Compendium
    Abbreviation
    Trends Biochem. Sci.
    Title
    Trends in Biochemical Sciences
    Publication Year
    1976-
    ISBN/ISSN
    0167-7640 0968-0004
    Data From Reference
    Genes (3)