Interferon-alpha-induced phosphorylation and activation of cytosolic phospholipase A2 is required for the formation of interferon-stimulated gene factor three.

Treatment of cells with interferon (IFN)-alpha caused phosphorylation and activation of cytosolic phospholipase A2 (cPLA2). The protein tyrosine kinase Jak1 was found to be necessary for the activation of cPLA2. Jak1 could be co-immunoprecipitated with cPLA2 from cell extracts, indicating that a close physical interaction occurs between these two proteins. ...
The induction of IFN-stimulated gene factor three (ISGF3) by IFN-alpha, is blocked by cPLA2 inhibitors in cell cultures and in cell-free reconstituted systems. However, these inhibitors do not block IFN-alpha or gamma-induced binding of STAT1 to the inverted repeat (IR) element of the IFN regulatory factor 1 (IRF-1) gene. Thus, cPLA2 activations occurs as an early event in the IFN-alpha response and is selectively involved in ISGF3-dependent gene activation.
Mesh Terms:
Base Sequence, Cytosol, DNA-Binding Proteins, Enzyme Activation, Gene Expression Regulation, HeLa Cells, Humans, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, gamma Subunit, Interferon-alpha, Interferon-gamma, Janus Kinase 1, Molecular Sequence Data, Mutation, Oligodeoxyribonucleotides, Phospholipases A, Phospholipases A2, Phosphorylation, Protein-Tyrosine Kinases, Recombinant Proteins, STAT1 Transcription Factor, Signal Transduction, Trans-Activators, Transcription Factors, Transcriptional Activation
EMBO J.
Date: Apr. 01, 1996
Download Curated Data For This Publication
162510
Switch View:
  • Interactions 2