Selective suppression of stress-activated protein kinase pathway by protein phosphatase 2C in mammalian cells.

@article{Hanada1998SelectiveSO,
  title={Selective suppression of stress-activated protein kinase pathway by protein phosphatase 2C in mammalian cells.},
  author={Masahito Hanada and Takayasu Kobayashi and Motoko Ohnishi and Satoshi Ikeda and Hongfeng Wang and Koji Katsura and Yuchio Yanagawa and Akira Hiraga and Ryunosuke Kanamaru and Shinri Tamura},
  journal={FEBS letters},
  year={1998},
  volume={437 3},
  pages={172-6}
}
Protein phosphatase 2Calpha (PP2Calpha) or PP2Cbeta-1 expressed in COS7 cells suppressed anisomycin- and NaCl-enhanced phosphorylations of p38 co-expressed in the cells. PP2Calpha or PP2Cbeta-1 expression also suppressed both basal and stress-enhanced phosphorylations of MKK3b and MKK6b, which are upstream protein kinases of p38, and of MKK4, which is one of the major upstream protein kinases of JNK. Basal activity of MKK7, another upstream protein kinase of JNK, was also suppressed by… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 29 extracted citations

Functional diversity of mammalian type 2C protein phosphatase isoforms: new tales from an old family.

Clinical and experimental pharmacology & physiology • 2008
View 3 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…