From the combination of knowledge and actions, someone can improve their skill and ability. It will lead them to live and work much better. This is why, the students, workers, or even employers should have reading habit for books. Any book will give certain knowledge to take all benefits. This is what this the interferon system tells you. It will add more knowledge of you to life and work better. Try it and prove it.

The Interferon System

A variety of neurotransmitters, hormones, and other regulatory agents affect the phosphorylation of specific proteins in their target tissues. The types of stimuli that share this common effect on protein phosphorylation include numerous substances that do not act through cyclic AMP. These and other observations suggest that many different classes of regulatory substances achieve certain of their biological effects by altering the phosphorylation of specific proteins.

http://science.sciencemag.org/content/sci/199/4325/146.full.pdf

Phosphorylated proteins as physiological effectors

Phosphorylation of initiation factor eIF-2 and the control of reticulocyte protein synthesis

This review describes the structure and function of the interferon (IFN)-inducible, double-stranded RNA-activated protein kinase PKR. This protein kinase has been studied extensively in recent years, and a large body of evidence has accumulated concerning its expression, interaction with regulatory RNA and protein molecules, and modes of activation and inhibition. PKR has been shown to play a variety of important roles in the regulation of translation, transcription, and signal transduction pathways through its ability to phosphorlate protein synthesis initiation factor eIF2, I-kB (the inhibitor of NF-kB), and other substrates. Expression studies involving both the wild-type protein and dominant negative mutants of PKR have established roles for the enzyme in the antiviral effects of IFNs, in the responses of uninfected cells to physiologic stresses, and in cell growth regulation. The possibility that PKR may function as a tumor suppressor and inducer of apoptosis suggests that this IFN-regulated protein ...

The double-stranded rna-dependent protein kinase pkr : structure and function

PROTEIN synthesis in cell-free systems from mouse L-cells pretreated with the antiviral agent interferon1 shows an enhanced sensitivity to inhibition by double-stranded RNA (dsRNA)2,3. The possible significance of this with respect to events in intact interferon-treated virus-infected cells has already been discussed2,4. We have already shown that the addition of small amounts of a post-ribosomal supernatant fraction from interferon-treated cells (interferon cell sap) renders protein synthesis in control cell-free systems sensitive to inhibition by dsRNA4. Our results are in accord with a two-step model involving an initial 100-fold activation of an inhibitor on incubation of the interferon cell sap with ATP and dsRNA (activation step), the activated inhibitor then interacting with the protein-synthetic system to inhibit translation (inhibitory step)5. In view of the dependence of the inhibition of protein synthesis upon incubation with ATP as well as dsRNA5 it was of interest to determine if a protein kinase(s) is involved, as seems to be the case in reticulocyte lysates in which phosphorylation of the initiator Met-tRNA binding factor (IF-E2) has been implicated following incubation of the lysates under a variety of inhibitory conditions including the presence of dsRNA (P. Farrell, K. Balkow, T. Hunt and R. J. Jackson, personal communication)6. In accord with this, we report here the presence of a dsRNA-dependent protein kinase activity in interferon cell sap. The inhibitor of protein synthesis which is activated on incubation of interferon cell sap with ATP and dsRNA, however, is heat stable and of relatively low molecular weight. It does not correspond either to the major polypeptide product of the interferon-dsRNA specific phosphorylation, or, presumably, to phosphorylated IF-E2.

Interferon-mediated protein kinase and low-molecular-weight inhibitor of protein synthesis

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2876%2980418-8

Perla Federman

Papers

Specific phosphorylation in vitro of a protein associated with ribosomes of interferon-treated mouse L cells.