Regulation of protein kinase cascades by protein phosphatase 2A.

Millward TA; Zolnierowicz S; Hemmings BA

doi:10.1016/s0968-0004(99)01375-4

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Journal article

Regulation of protein kinase cascades by protein phosphatase 2A.

Millward TA Friedrich Miescher-Institut, Maulbeerstrasse 66, CH-4058 Basel, Switzerland.
Zolnierowicz S
Hemmings BA

1999-05-14

Published in:

Trends in biochemical sciences. - 1999

Calcium-Calmodulin-Dependent Protein Kinases

Dual Specificity Phosphatase 1

Protein-Serine-Threonine Kinases

English 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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