Activation of Protein Kinase Cδ by IFN-γ | Zendy

Dilip K. Deb | Zendy; Antonella Sassano | Zendy; Fatima Lekmine | Zendy; Beata Majchrzak | Zendy; Amit Verma | Zendy; Suman Kambhampati | Zendy; Shahab Uddin | Zendy; Arshad Rahman | Zendy; Eleanor N. Fish | Zendy; Leonidas C. Platanias | Zendy

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Activation of Protein Kinase Cδ by IFN-γ

Author(s) -

Dilip K. Deb,

Antonella Sassano,

Fatima Lekmine,

Beata Majchrzak,

Amit Verma,

Suman Kambhampati,

Shahab Uddin,

Arshad Rahman,

Eleanor N. Fish,

Leonidas C. Platanias

Publication year - 2003

Publication title -

the journal of immunology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.737

H-Index - 372

eISSN - 1550-6606

pISSN - 0022-1767

DOI - 10.4049/jimmunol.171.1.267

Subject(s) - stat1 , map kinase kinase kinase , protein kinase c , phosphorylation , ask1 , map2k7 , microbiology and biotechnology , casein kinase 2 , chemistry , interleukin 13 receptor , mitogen activated protein kinase kinase , cyclin dependent kinase 9 , c raf , signal transduction , janus kinase 1 , protein kinase a , cyclin dependent kinase 2 , biology , janus kinase , biochemistry , receptor , insulin like growth factor 1 receptor , growth factor

Engagement of the type II IFN (IFN-gamma) receptor results in activation of the Janus kinase-Stat pathway and induction of gene transcription via IFN-gamma-activated site (GAS) elements in the promoters of IFN-gamma-inducible genes. An important event in IFN-gamma-dependent gene transcription is phosphorylation of Stat1 on Ser(727), which is regulated by a kinase activated downstream of the phosphatidylinositol 3'-kinase. Here we provide evidence that a member of the protein kinase C (PKC) family of proteins is activated downstream of the phosphatidylinositol 3'-kinase and is engaged in IFN-gamma signaling. Our data demonstrate that PKCdelta is rapidly phosphorylated during engagement of the type II IFNR and its kinase domain is induced. Subsequently, the activated PKCdelta associates with a member of the Stat family of proteins, Stat1, which acts as a substrate for its kinase activity and undergoes phosphorylation on Ser(727). Inhibition of PKCdelta activity diminishes phosphorylation of Stat1 on Ser(727) and IFN-gamma-dependent transcriptional regulation via IFN-gamma-activated site elements, without affecting the phosphorylation of the protein on Tyr(701). Thus, PKCdelta is activated during engagement of the IFN-gamma receptor and plays an important role in IFN-gamma signaling by mediating serine phosphorylation of Stat1 and facilitating transcription of IFN-gamma-stimulated genes.

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