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Regulation of protein kinase cascades by protein phosphatase 2A.

Authors
  • Millward, T A
  • Zolnierowicz, S
  • Hemmings, B A
Type
Published Article
Journal
Trends in Biochemical Sciences
Publisher
Elsevier
Publication Date
May 01, 1999
Volume
24
Issue
5
Pages
186–191
Identifiers
PMID: 10322434
Source
Medline
License
Unknown

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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