Regulation of stress-activated protein kinase signaling pathways by protein phosphatases

Shinri Tamura, Masahito Hanada, Motoko Ohnishi, Koji Katsura, Masato Sasaki, Takayasu Kobayashi

Research output: Contribution to journalShort surveypeer-review

92 Citations (Scopus)


Stress-activated protein kinase (SAPK) signaling plays essential roles in eliciting adequate cellular responses to stresses and proinflammatory cytokines. SAPK pathways are composed of three successive protein kinase reactions. The phosphorylation of SAPK signaling components on Ser/Thr or Thr/Tyr residues suggests the involvement of various protein phosphatases in the negative regulation of these systems. Accumulating evidence indicates that three families of protein phosphatases, namely the Ser/Thr phosphatases, the Tyr phosphatases and the dual specificity Ser/Thr/Tyr phosphatases regulate these pathways, each mediating a distinct function. Differences in substrate specificities and regulatory mechanisms for these phosphatases form the molecular basis for the complex regulation of SAPK signaling. Here we describe the properties of the protein phosphatases responsible for the regulation of SAPK signaling pathways.

Original languageEnglish
Pages (from-to)1060-1066
Number of pages7
JournalEuropean Journal of Biochemistry
Issue number4
Publication statusPublished - 2002


  • Protein phosphatase
  • Stress response
  • Stress-activated protein kinase


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