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Double‐stranded RNA‐activated protein kinase interacts with apoptosis signal‐regulating kinase 1: Implications for apoptosis signaling pathways by Takenori Takizawa; Chizuru Tatematsu; Yoshinobu Nakanishi is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Double‐stranded RNA‐activated protein kinase (PKR), a serine/threonine kinase, is activated in virus‐infected cells and acts as an antiviral machinery of type I interferons. PKR controls several stress response pathways induced by double‐stranded RNA, tumor necrosis factor‐α or lipopolysaccharide, which result in the activation of stress‐activated protein kinase/c‐Jun NH~2~‐terminal kinase and p38 of the mitogen‐activated protein kinase family. Here we showed a novel interaction between PKR and apoptosis signal‐regulating kinase 1 (ASK1), one of the members of the mitogen‐activated protein kinase kinase kinase family, which is activated in response to a variety of apoptosis‐inducing stimuli. PKR and ASK1 showed predominant cytoplasmic localization in COS‐1 cells transfected with both cDNAs, and coimmunoprecipitated from the cell extracts. A dominant negative mutant of PKR (PKR‐KR) inhibited both the apoptosis and p38 activation induced by ASK1 __in vivo__. Consistently, PKR‐KR inhibited the autophosphorylation of ASK1 __in vitro__, and exposure to poly(I)–poly(C) increased the phosphorylation of ASK1 __in vivo__. These results indicate the existence of a link between PKR and ASK1,

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Author

Takenori Takizawa; Chizuru Tatematsu; Yoshinobu Nakanishi

Publisher

John Wiley and Sons; Springer; Wiley (Blackwell Publishing); Springer-Verlag; Blackwell Publishing Inc.; Springer Verlag; Wiley; Springer Science and Business Media LLC (ISSN 1432-1327)

Published

2002

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)