Open AccessRegulation of stress‐activated protein kinase signaling pathways by protein phosphatases
Author(s) -
Tamura Shinri,
Hanada Masahito,
Ohnishi Motoko,
Katsura Koji,
Sasaki Masato,
Kobayashi Takayasu
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.0014-2956.2002.02754.x
Subject(s) - ask1 , phosphatase , protein kinase a , microbiology and biotechnology , signal transduction , kinase , c raf , protein phosphatase 2 , mitogen activated protein kinase kinase , chemistry , phosphorylation , biology
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.